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| - | [[Image:1hv9.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1hv9| PDB=1hv9 | SCENE= }} | | {{STRUCTURE_1hv9| PDB=1hv9 | SCENE= }} |
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| - | '''STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES'''
| + | ===STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES=== |
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| - | ==Overview==
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| - | N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU) is a trimeric bifunctional enzyme that catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. The X-ray crystal structure of Escherichia coli GlmU in complex with UDP-GlcNAc and CoA has been determined to 2.1 A resolution and reveals a two-domain architecture that is responsible for these two reactions. The C-terminal domain is responsible for the CoA-dependent acetylation of Glc-1-PO(4) to GlcNAc-1-PO(4) and displays the longest left-handed parallel beta-helix observed to date. The acetyltransferase active site defined by the binding site for CoA makes use of residues from all three subunits and is positioned beneath an open cavity large enough to accommodate the Glc-1-PO(4) acetyl acceptor. The N-terminal domain catalyzes uridyl transfer from UTP to GlcNAc-1-PO(4) to form the final products UDP-GlcNAc and pyrophosphate. This domain is composed of a central seven-stranded beta-sheet surrounded by six alpha-helices in a Rossmann fold-like topology. A Co(2+) ion binds to just one of the two independent pyrophosphorylase active sites present in the crystals studied here, each of which nonetheless binds UDP-GlcNAc. The conformational changes of the enzyme and sugar nucleotide that accompany metal binding may provide a window into the structural dynamics that accompany catalysis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11329257}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11329257 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11329257}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Roderick, S L.]] | | [[Category: Roderick, S L.]] |
| | [[Category: Left-handed parallel beta-helix]] | | [[Category: Left-handed parallel beta-helix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:16:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:50:27 2008'' |
Revision as of 05:50, 1 July 2008
Template:STRUCTURE 1hv9
STRUCTURE OF E. COLI GLMU: ANALYSIS OF PYROPHOSPHORYLASE AND ACETYLTRANSFERASE ACTIVE SITES
Template:ABSTRACT PUBMED 11329257
About this Structure
1HV9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites., Olsen LR, Roderick SL, Biochemistry. 2001 Feb 20;40(7):1913-21. PMID:11329257
Page seeded by OCA on Tue Jul 1 08:50:27 2008
