1upa

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(New page: 200px<br /> <applet load="1upa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1upa, resolution 2.35&Aring;" /> '''CARBOXYETHYLARGININ...)
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==About this Structure==
==About this Structure==
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1UPA 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]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UPA OCA]].
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1UPA 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UPA OCA]].
==Reference==
==Reference==
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[[Category: lactamase]]
[[Category: lactamase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:29:23 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:20:46 2007''

Revision as of 11:16, 30 October 2007


1upa, resolution 2.35Å

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CARBOXYETHYLARGININE SYNTHASE FROM STREPTOMYCES CLAVULIGERUS (SEMET STRUCTURE)

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, ... [(full description)]

About this Structure

1UPA is a [Single protein] structure of sequence from [Streptomyces clavuligerus] with MG, SO4 and TPP as [ligands]. Structure known Active Site: AC1. 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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