2oi5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The biosynthesis of UDP-GlcNAc in bacteria is carried out by GlmU, an | + | The biosynthesis of UDP-GlcNAc in bacteria is carried out by GlmU, an essential bifunctional uridyltransferase that catalyzes the CoA-dependent acetylation of GlcN-1-PO(4) to form GlcNAc-1-PO(4) and its subsequent condensation with UTP to form pyrophosphate and UDP-GlcNAc. As a metabolite, UDP-GlcNAc is situated at a branch point leading to the biosynthesis of lipopolysaccharide and peptidoglycan. Consequently, GlmU is regarded as an important target for potential antibacterial agents. The crystal structure of the Escherichia coli GlmU acetyltransferase active site has been determined in complexes with acetyl-CoA, CoA/GlcN-1-PO(4), and desulpho-CoA/GlcNAc-1-PO(4). These structures reveal the enzyme groups responsible for binding the substrates. A superposition of these complex structures suggests that the 2-amino group of GlcN-1-PO(4) is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Olsen, L | + | [[Category: Olsen, L R.]] |
| - | [[Category: Roderick, S | + | [[Category: Roderick, S L.]] |
| - | [[Category: Vetting, M | + | [[Category: Vetting, M W.]] |
[[Category: ACO]] | [[Category: ACO]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: left-handed beta helix]] | [[Category: left-handed beta helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:18:49 2008'' |
Revision as of 16:18, 21 February 2008
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E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA
Overview
The biosynthesis of UDP-GlcNAc in bacteria is carried out by GlmU, an essential bifunctional uridyltransferase that catalyzes the CoA-dependent acetylation of GlcN-1-PO(4) to form GlcNAc-1-PO(4) and its subsequent condensation with UTP to form pyrophosphate and UDP-GlcNAc. As a metabolite, UDP-GlcNAc is situated at a branch point leading to the biosynthesis of lipopolysaccharide and peptidoglycan. Consequently, GlmU is regarded as an important target for potential antibacterial agents. The crystal structure of the Escherichia coli GlmU acetyltransferase active site has been determined in complexes with acetyl-CoA, CoA/GlcN-1-PO(4), and desulpho-CoA/GlcNAc-1-PO(4). These structures reveal the enzyme groups responsible for binding the substrates. A superposition of these complex structures suggests that the 2-amino group of GlcN-1-PO(4) is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism.
About this Structure
2OI5 is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products., Olsen LR, Vetting MW, Roderick SL, Protein Sci. 2007 Jun;16(6):1230-5. Epub 2007 May 1. PMID:17473010
Page seeded by OCA on Thu Feb 21 18:18:49 2008
Categories: Escherichia coli | Single protein | Olsen, L R. | Roderick, S L. | Vetting, M W. | ACO | MG | SO4 | UD1 | Left-handed beta helix
