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| | <StructureSection load='2v8h' size='340' side='right'caption='[[2v8h]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='2v8h' size='340' side='right'caption='[[2v8h]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v8h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_58438 Atcc 58438]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V8H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v8h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lachancea_kluyveri Lachancea kluyveri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V8H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=URP:N-(AMINOCARBONYL)-BETA-ALANINE'>URP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2v8v|2v8v]], [[2v8d|2v8d]], [[2v8g|2v8g]], [[1r43|1r43]], [[1r3n|1r3n]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=URP:N-(AMINOCARBONYL)-BETA-ALANINE'>URP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ureidopropionase Beta-ureidopropionase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.6 3.5.1.6] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v8h OCA], [https://pdbe.org/2v8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v8h RCSB], [https://www.ebi.ac.uk/pdbsum/2v8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v8h ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v8h OCA], [https://pdbe.org/2v8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v8h RCSB], [https://www.ebi.ac.uk/pdbsum/2v8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v8h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q96W94_LACKL Q96W94_LACKL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 58438]] | + | [[Category: Lachancea kluyveri]] |
| - | [[Category: Beta-ureidopropionase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andersen, B]] | + | [[Category: Andersen B]] |
| - | [[Category: Dobritzsch, D]] | + | [[Category: Dobritzsch D]] |
| - | [[Category: Lundgren, S]] | + | [[Category: Lundgren S]] |
| - | [[Category: Piskur, J]] | + | [[Category: Piskur J]] |
| - | [[Category: Alpha and beta protein]]
| + | |
| - | [[Category: Amidohydrolase]]
| + | |
| - | [[Category: Complex with n-carbamyl-beta-alanine]]
| + | |
| - | [[Category: Di-zinc center]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q96W94_LACKL
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lundgren S, Andersen B, Piskur J, Dobritzsch D. Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements. J Biol Chem. 2007 Dec 7;282(49):36037-47. Epub 2007 Oct 4. PMID:17916556 doi:http://dx.doi.org/10.1074/jbc.M705517200
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