(Q27644659)

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Structure of theE. colibifunctional GlmU acetyltransferase active site with substrates and products

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title

Structure of theE. colibifunctional GlmU acetyltransferase active site with substrates and products (English)

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author name string

Laurence R Olsen

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1

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Matthew W Vetting

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2

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Steven L Roderick

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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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page(s)

1230-5

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issue

6

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cites work

Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites

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PubMed Central

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20 March 2017

Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution

1 reference

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PubMed Central

reference URL

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20 March 2017

Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture

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PubMed Central

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20 March 2017

Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily

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PubMed Central

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20 March 2017

Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli

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20 March 2017

A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase

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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

Improved methods for building protein models in electron density maps and the location of errors in these models

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20 March 2017

Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase

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PubMed Central

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29 September 2017

Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes

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29 September 2017

Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli

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29 September 2017

Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli.

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29 September 2017

What is known about the structure and function of the Escherichia coli protein FirA?

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29 September 2017

Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme

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PubMed Central

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2 June 2018

Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acyltransferase that converts UDP-N-acetylglucosamine to UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine

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reference URL

https://pubmed.ncbi.nlm.nih.gov/17473010

retrieved

12 December 2020

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6357049

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(Q27644659)

Structure of theE. colibifunctional GlmU acetyltransferase active site with substrates and products

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