(Q27639672)

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Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

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title

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA (English)

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author

Johann Deisenhofer

series ordinal

7

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author name string

John F Hunt

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1

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Sevil Weinkauf

series ordinal

2

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Lisa Henry

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3

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John J Fak

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4

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Paul McNicholas

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5

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Donald B Oliver

series ordinal

6

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language of work or name

English

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publication date

20 September 2002

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published in

Science

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volume

297

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issue

5589

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page(s)

2018-26

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cites work

Secretion monitor, SecM, undergoes self-translation arrest in the cytosol

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Modularity and specialization in superfamily 1 and 2 helicases

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Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation

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11 October 2022

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SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

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Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii

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11 October 2022

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Miscellaneous algorithms for density modification

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https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Conformational stabilization and crystallization of the SecA translocation ATPase from Bacillus subtilis

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11 October 2022

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Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Domain interactions of the peripheral preprotein Translocase subunit SecA.

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Nucleotide binding activity of SecA homodimer is conformationally regulated by temperature and altered by prlD and azi mutations

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Dali: a network tool for protein structure comparison

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Identification of elements on GeneX-secA RNA of Escherichia coli required for SecA binding and secA auto-regulation.

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

The C terminus of SecA is involved in both lipid binding and SecB binding.

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Integration of SecA protein into the Escherichia coli inner membrane is regulated by its amino-terminal ATP-binding domain

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Thermodynamics of nucleotide binding to NBS-I of the Bacillus subtilis preprotein translocase subunit SecA

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Carboxy-terminal region of Escherichia coli SecA ATPase is important to promote its protein translocation activity in vivo.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Escherichia coli SecA shape and dimensions

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Zinc stabilizes the SecB binding site of SecA.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Genetic dissection of SecA: suppressor mutations against the secY205 translocase defect

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Complex behavior in solution of homodimeric SecA.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

The high affinity ATP binding site modulates the SecA-precursor interaction

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Interaction between SecA and SecYEG in Micellar Solution and Formation of the Membrane-Inserted State†

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in secA

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

The structural basis of protein targeting and translocation in bacteria.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Lipid and signal peptide-induced conformational changes within the C-domain of Escherichia coli SecA protein

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Identification of a region of interaction between Escherichia coli SecA and SecY proteins.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Helicase structure and mechanism

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

Stability and solvent accessibility of SecA protein of Escherichia coli

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1126/SCIENCE.1074424

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10.1126/SCIENCE.1074424

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(Q27639672)

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

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