1r3n: Difference between revisions

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New page: left|200px<br /><applet load="1r3n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r3n, resolution 2.70Å" /> '''Crystal structure of...
 
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[[Image:1r3n.gif|left|200px]]<br /><applet load="1r3n" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1r3n, resolution 2.70&Aring;" />
'''Crystal structure of beta-alanine synthase from Saccharomyces kluyveri'''<br />


==Overview==
==Crystal structure of beta-alanine synthase from Saccharomyces kluyveri==
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.
<StructureSection load='1r3n' size='340' side='right'caption='[[1r3n]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1r3n]] is a 8 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=1R3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R3N FirstGlance]. <br>
1R3N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lachancea_kluyveri Lachancea kluyveri] with ZN and BIB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R3N OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r3n OCA], [https://pdbe.org/1r3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r3n RCSB], [https://www.ebi.ac.uk/pdbsum/1r3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r3n ProSAT]</span></td></tr>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14534321 14534321]
</table>
[[Category: Beta-ureidopropionase]]
== Function ==
[https://www.uniprot.org/uniprot/Q96W94_LACKL Q96W94_LACKL]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r3/1r3n_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r3n ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Lachancea kluyveri]]
[[Category: Lachancea kluyveri]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dobritzsch, D.]]
[[Category: Dobritzsch D]]
[[Category: Gojkovic, Z.]]
[[Category: Gojkovic Z]]
[[Category: Lundgren, S.]]
[[Category: Lundgren S]]
[[Category: Piskur, J.]]
[[Category: Piskur J]]
[[Category: BIB]]
[[Category: ZN]]
[[Category: alpha and beta protein]]
[[Category: di-zinc center]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:03:14 2007''

Latest revision as of 08:20, 14 February 2024

Crystal structure of beta-alanine synthase from Saccharomyces kluyveri

1r3n, resolution 2.70Å

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