2v8d: Difference between revisions

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[[Image:2v8d.gif|left|200px]]
{{Seed}}
[[Image:2v8d.png|left|200px]]


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{{STRUCTURE_2v8d|  PDB=2v8d  |  SCENE=  }}  
{{STRUCTURE_2v8d|  PDB=2v8d  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF MUTANT E159A OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI'''
===CRYSTAL STRUCTURE OF MUTANT E159A OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI===




==Overview==
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Beta-alanine synthase is the final enzyme of the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of uracil and thymine in higher organisms. The fold of the homodimeric enzyme from the yeast Saccharomyces kluyveri identifies it as a member of the AcyI/M20 family of metallopeptidases. Its subunit consists of a catalytic domain harboring a di-zinc center and a smaller dimerization domain. The present site-directed mutagenesis studies identify Glu(159) and Arg(322) as crucial for catalysis and His(262) and His(397) as functionally important but not essential. We determined the crystal structures of wild-type beta-alanine synthase in complex with the reaction product beta-alanine, and of the mutant E159A with the substrate N-carbamyl-beta-alanine, revealing the closed state of a dimeric AcyI/M20 metallopeptidase-like enzyme. Subunit closure is achieved by a approximately 30 degrees rigid body domain rotation, which completes the active site by integration of substrate binding residues that belong to the dimerization domain of the same or the partner subunit. Substrate binding is achieved via a salt bridge, a number of hydrogen bonds, and coordination to one of the zinc ions of the di-metal center.
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{{ABSTRACT_PUBMED_17916556}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements., Lundgren S, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17916556 17916556]
Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements., Lundgren S, Andersen B, Piskur J, Dobritzsch D, J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17916556 17916556]
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:[http://www.ncbi.nlm.nih.gov/pubmed/14534321 14534321]
Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri., Dobritzsch D, Gojkovic Z, Andersen B, Piskur J, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1267-9. Epub 2003, Jun 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12832781 12832781]
[[Category: Beta-ureidopropionase]]
[[Category: Beta-ureidopropionase]]
[[Category: Lachancea kluyveri]]
[[Category: Lachancea kluyveri]]
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[[Category: Di-zinc center]]
[[Category: Di-zinc center]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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