(Q27644662)

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Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+complex reveals a novel cofactor binding mode

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Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+complex reveals a novel cofactor binding mode (English)

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author name string

N Divya

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1

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E Grifith

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2

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Narendra Narayana

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3

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publication date

June 2007

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published in

Protein Science

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volume

16

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issue

6

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page(s)

1063-8

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cites work

A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site

1 reference

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PubMed Central

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20 March 2017

Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state

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PubMed Central

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20 March 2017

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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20 March 2017

The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins

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20 March 2017

Searching sequence space: two different approaches to dihydrofolate reductase catalysis

1 reference

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PubMed Central

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29 September 2017

Interactive electron-density map interpretation: from INTER to O.

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PubMed Central

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29 September 2017

Unusual binding stoichiometries and cooperativity are observed during binary and ternary complex formation in the single active pore of R67 dihydrofolate reductase, a D2 symmetric protein

1 reference

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PubMed Central

reference URL

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29 September 2017

Crystal structure of a novel trimethoprim-resistant dihydrofolate reductase specified in Escherichia coli by R-plasmid R67.

1 reference

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PubMed Central

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29 September 2017

Conformation of NADP+ bound to a type II dihydrofolate reductase.

1 reference

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PubMed Central

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2 June 2018

High-resolution structure of a plasmid-encoded dihydrofolate reductase: pentagonal network of water molecules in the D2-symmetric active site.

1 reference

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2206676

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27 November 2018

Role of ionic interactions in ligand binding and catalysis of R67 dihydrofolate reductase

1 reference

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PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2206676

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27 November 2018

Interligand Overhauser effects in type II dihydrofolate reductase

1 reference

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PubMed Central

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27 November 2018

Titration of histidine 62 in R67 dihydrofolate reductase is linked to a tetramer<-->two-dimer equilibrium.

1 reference

stated in

PubMed Central

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2206676

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27 November 2018

Trimethoprim resistance determined by R factors

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/17473013

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A glutamine 67--> histidine mutation in homotetrameric R67 dihydrofolate reductase results in four mutations per single active site pore and causes substantial substrate and cofactor inhibition

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/17473013

retrieved

12 December 2020

based on heuristic

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PubMed publication ID

17473013

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ResearchGate publication ID

6357052

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(Q27644662)

Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+complex reveals a novel cofactor binding mode

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