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| [[Image:1g95.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1g95| PDB=1g95 | SCENE= }} | | {{STRUCTURE_1g95| PDB=1g95 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF S.PNEUMONIAE GLMU, APO FORM'''
| | ===CRYSTAL STRUCTURE OF S.PNEUMONIAE GLMU, APO FORM=== |
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| ==Overview==
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| N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU) is an essential bacterial enzyme with both an acetyltransferase and a uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways. GlmU is therefore an attractive target for potential antibiotics. Knowledge of its three-dimensional structure would provide a basis for rational drug design. We have determined the crystal structures of Streptococcus pneumoniae GlmU (SpGlmU) in apo form at 2.33 A resolution, and in complex with UDP-N-acetyl glucosamine and the essential co-factor Mg(2+) at 1.96 A resolution. The protein structure consists of an N-terminal domain with an alpha/beta-fold, containing the uridyltransferase active site, and a C-terminal domain with a long left-handed beta-sheet helix (LbetaH) domain. An insertion loop containing the highly conserved sequence motif Asn-Tyr-Asp-Gly protrudes from the left-handed beta-sheet helix domain. In the crystal, S. pneumoniae GlmU forms exact trimers, mainly through contacts between left-handed beta-sheet helix domains. UDP-N-acetylglucosamine and Mg(2+) are bound at the uridyltransferase active site, which is in a closed form. We propose a uridyltransferase mechanism in which the activation energy of the double negatively charged phosphorane transition state is lowered by charge compensation of Mg(2+) and the side-chain of Lys22.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11124906}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11124906 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11124906}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Trimer]] | | [[Category: Trimer]] |
| [[Category: Uridyltransferase pyrophosphorylase]] | | [[Category: Uridyltransferase pyrophosphorylase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:18:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:54:52 2008'' |
