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| - | [[Image:1g97.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1g97| PDB=1g97 | SCENE= }} | | {{STRUCTURE_1g97| PDB=1g97 | SCENE= }} |
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| - | '''S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+'''
| + | ===S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+=== |
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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: Udp-n-acetylglucosamine]] | | [[Category: Udp-n-acetylglucosamine]] |
| | [[Category: Uridyltransferase]] | | [[Category: Uridyltransferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:18:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:55:45 2008'' |
Revision as of 01:55, 1 July 2008
Template:STRUCTURE 1g97
S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+
Template:ABSTRACT PUBMED 11124906
About this Structure
1G97 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.
Reference
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., Kostrewa D, D'Arcy A, Takacs B, Kamber M, J Mol Biol. 2001 Jan 12;305(2):279-89. PMID:11124906
Page seeded by OCA on Tue Jul 1 04:55:45 2008
