1g97
From Proteopedia
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|PDB= 1g97 |SIZE=350|CAPTION= <scene name='initialview01'>1g97</scene>, resolution 1.96Å | |PDB= 1g97 |SIZE=350|CAPTION= <scene name='initialview01'>1g97</scene>, resolution 1.96Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1g95|1G95]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g97 OCA], [http://www.ebi.ac.uk/pdbsum/1g97 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g97 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kamber, M.]] | [[Category: Kamber, M.]] | ||
[[Category: Kostrewa, D.]] | [[Category: Kostrewa, D.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: UD1]] | ||
[[Category: acetyltransferase]] | [[Category: acetyltransferase]] | ||
[[Category: glmu]] | [[Category: glmu]] | ||
| Line 38: | Line 38: | ||
[[Category: uridyltransferase]] | [[Category: uridyltransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:39:18 2008'' |
Revision as of 17:39, 30 March 2008
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| , resolution 1.96Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | UDP-N-acetylglucosamine diphosphorylase, with EC number 2.7.7.23 | ||||||
| Related: | 1G95
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
S.PNEUMONIAE GLMU COMPLEXED WITH UDP-N-ACETYLGLUCOSAMINE AND MG2+
Overview
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.
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
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