1upc
From Proteopedia
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| - | [[Image:1upc. | + | [[Image:1upc.jpg|left|200px]]<br /><applet load="1upc" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1upc" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1upc, resolution 2.45Å" /> | caption="1upc, resolution 2.45Å" /> | ||
'''CARBOXYETHYLARGININE SYNTHASE FROM STREPTOMYCES CLAVULIGERUS'''<br /> | '''CARBOXYETHYLARGININE SYNTHASE FROM STREPTOMYCES CLAVULIGERUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus] with MG, SO4 and TPP as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 1UPC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus] with MG, SO4 and TPP as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain F'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UPC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thiamine pyrophosphate]] | [[Category: thiamine pyrophosphate]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:06:18 2007'' |
Revision as of 15:56, 18 December 2007
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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 with MG, SO4 and TPP as ligands. Known structural/functional Site: . 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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