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1r43

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{{STRUCTURE_1r43| PDB=1r43 | SCENE= }}
{{STRUCTURE_1r43| PDB=1r43 | SCENE= }}
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'''Crystal structure of beta-alanine synthase from Saccharomyces kluyveri (selenomethionine substituted protein)'''
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===Crystal structure of beta-alanine synthase from Saccharomyces kluyveri (selenomethionine substituted protein)===
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==Overview==
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beta-Alanine synthase (beta AS) is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of pyrimidine bases, including several anticancer drugs. In eukaryotes, beta ASs belong to two subfamilies, which exhibit a low degree of sequence similarity. We determined the structure of beta AS from Saccharomyces kluyveri to a resolution of 2.7 A. The subunit of the homodimeric enzyme consists of two domains: a larger catalytic domain with a dizinc metal center, which represents the active site of beta AS, and a smaller domain mediating the majority of the intersubunit contacts. Both domains exhibit a mixed alpha/beta-topology. Surprisingly, the observed high structural homology to a family of dizinc-dependent exopeptidases suggests that these two enzyme groups have a common origin. Alterations in the ligand composition of the metal-binding site can be explained as adjustments to the catalysis of a different reaction, the hydrolysis of an N-carbamyl bond by beta AS compared with the hydrolysis of a peptide bond by exopeptidases. In contrast, there is no resemblance to the three-dimensional structure of the functionally closely related N-carbamyl-d-amino acid amidohydrolases. Based on comparative structural analysis and observed deviations in the backbone conformations of the eight copies of the subunit in the asymmetric unit, we suggest that conformational changes occur during each catalytic cycle.
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(as it appears on PubMed at http://www.pubmed.gov), where 14534321 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14534321}}
==About this Structure==
==About this Structure==
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[[Category: Alpha and beta protein]]
[[Category: Alpha and beta protein]]
[[Category: One di-zinc center per subunit]]
[[Category: One di-zinc center per subunit]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:02:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:38:18 2008''

Revision as of 10:38, 27 July 2008

Image:1r43.png

Template:STRUCTURE 1r43

Crystal structure of beta-alanine synthase from Saccharomyces kluyveri (selenomethionine substituted protein)

Template:ABSTRACT PUBMED 14534321

About this Structure

1R43 is a Single protein structure of sequence from Lachancea kluyveri. Full crystallographic information is available from OCA.

Reference

Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases., Lundgren S, Gojkovic Z, Piskur J, Dobritzsch D, J Biol Chem. 2003 Dec 19;278(51):51851-62. Epub 2003 Oct 8. PMID:14534321

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