1upc
From Proteopedia
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|PDB= 1upc |SIZE=350|CAPTION= <scene name='initialview01'>1upc</scene>, resolution 2.45Å | |PDB= 1upc |SIZE=350|CAPTION= <scene name='initialview01'>1upc</scene>, resolution 2.45Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+F'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+F'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1upc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1upc OCA], [http://www.ebi.ac.uk/pdbsum/1upc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1upc RCSB]</span> | ||
}} | }} | ||
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[[Category: Hewitson, K S.]] | [[Category: Hewitson, K S.]] | ||
[[Category: Schofield, C J.]] | [[Category: Schofield, C J.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: TPP]] | ||
[[Category: antibiotic]] | [[Category: antibiotic]] | ||
[[Category: clavulanic acid]] | [[Category: clavulanic acid]] | ||
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[[Category: thiamine pyrophosphate]] | [[Category: thiamine pyrophosphate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:13:31 2008'' |
Revision as of 21:13, 30 March 2008
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| , resolution 2.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CARBOXYETHYLARGININE SYNTHASE FROM STREPTOMYCES CLAVULIGERUS
Overview
The initial step in the biosynthesis of the clinically important beta-lactamase inhibitor clavulanic acid involves condensation of two primary metabolites, D-glyceraldehyde 3-phosphate and L-arginine, to give N2-(2-carboxyethyl)arginine, a beta-amino acid. This unusual N-C bond forming reaction is catalyzed by the thiamin diphosphate (ThP2)-dependent enzyme N2-(2-carboxyethyl)arginine synthase. Here we report the crystal structure of N2-(2-carboxyethyl)arginine synthase, complexed with ThP2 and Mg2+, to 2.35-A resolution. The structure was solved in two space groups, P2(1)2(1)2(1) and P2(1)2(1)2. In both, the enzyme is observed in a tetrameric form, composed of a dimer of two more tightly associated dimers, consistent with both mass spectrometric and gel filtration chromatography studies. Both ThP2 and Mg2+ cofactors are present at the active site, with ThP2 in a "V" conformation as in related enzymes. A sulfate anion is observed in the active site of the enzyme in a location proposed as a binding site for the phosphate group of the d-glyceraldehyde 3-phosphate substrate. The mechanistic implications of the active site arrangement are discussed, including the potential role of the aminopyrimidine ring of the ThP2. The structure will form a basis for future mechanistic and structural studies, as well as engineering aimed at production of alternative beta-amino acids.
About this Structure
1UPC is a Single protein structure of sequence from Streptomyces clavuligerus. Full crystallographic information is available from OCA.
Reference
Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway., Caines ME, Elkins JM, Hewitson KS, Schofield CJ, J Biol Chem. 2004 Feb 13;279(7):5685-92. Epub 2003 Nov 17. PMID:14623876
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