1upc
From Proteopedia
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| - | [[Image:1upc.jpg|left|200px]] | + | [[Image:1upc.jpg|left|200px]] |
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| - | '''CARBOXYETHYLARGININE SYNTHASE FROM STREPTOMYCES CLAVULIGERUS''' | + | {{Structure |
| + | |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> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=TPP:THIAMINE DIPHOSPHATE'>TPP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CARBOXYETHYLARGININE SYNTHASE FROM STREPTOMYCES CLAVULIGERUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UPC is a [ | + | 1UPC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UPC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14623876 14623876] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces clavuligerus]] | [[Category: Streptomyces clavuligerus]] | ||
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[[Category: thiamine pyrophosphate]] | [[Category: thiamine pyrophosphate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:35:04 2008'' |
Revision as of 12:35, 20 March 2008
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| , resolution 2.45Å | |||||||
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| Sites: | |||||||
| Ligands: | , and | ||||||
| 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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