2v8v
From Proteopedia
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| - | [[Image:2v8v.gif|left|200px]] | + | [[Image:2v8v.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF MUTANT R322A OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI''' | + | {{Structure |
| + | |PDB= 2v8v |SIZE=350|CAPTION= <scene name='initialview01'>2v8v</scene>, resolution 2.90Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Urp+Binding+Site+For+Chain+B'>AC5</scene>, <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+C'>AC6</scene>, <scene name='pdbsite=AC7:Zn+Binding+Site+For+Chain+C'>AC7</scene>, <scene name='pdbsite=AC8:Dtt+Binding+Site+For+Chain+C'>AC8</scene>, <scene name='pdbsite=AC9:Urp+Binding+Site+For+Chain+C'>AC9</scene>, <scene name='pdbsite=BC1:Zn+Binding+Site+For+Chain+D'>BC1</scene>, <scene name='pdbsite=BC2:Zn+Binding+Site+For+Chain+D'>BC2</scene> and <scene name='pdbsite=BC3:Urp+Binding+Site+For+Chain+D'>BC3</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=URP:N-(AMINOCARBONYL)-BETA-ALANINE'>URP</scene> and <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-ureidopropionase Beta-ureidopropionase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.6 3.5.1.6] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF MUTANT R322A OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2V8V is a [ | + | 2V8V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lachancea_kluyveri Lachancea kluyveri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V8V OCA]. |
==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:// | + | 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] |
[[Category: Beta-ureidopropionase]] | [[Category: Beta-ureidopropionase]] | ||
[[Category: Lachancea kluyveri]] | [[Category: Lachancea kluyveri]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 18:44:19 2008'' |
Revision as of 16:44, 20 March 2008
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| , resolution 2.90Å | |||||||
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| Sites: | , , , , , , , , , , and | ||||||
| Ligands: | , and | ||||||
| Activity: | Beta-ureidopropionase, with EC number 3.5.1.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MUTANT R322A OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI
Overview
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.
About this Structure
2V8V is a Single protein structure of sequence from Lachancea kluyveri. Full crystallographic information is available from OCA.
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:17916556
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