1r3n

<table><tr><td colspan='2'>[[1r3n]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_58438 Atcc 58438]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R3N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R3N FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BIB:BETA-AMINO+ISOBUTYRATE'>BIB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r43|1r43]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYD3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4934 ATCC 58438])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r3n OCA], [http://pdbe.org/1r3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r3n RCSB], [http://www.ebi.ac.uk/pdbsum/1r3n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r3n ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:14534321</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 58438]]

[[Category: Beta-ureidopropionase]]

[[Category: Dobritzsch, D]]

[[Category: Gojkovic, Z]]

[[Category: Lundgren, S]]

[[Category: Piskur, J]]

[[Category: Hydrolase]]