2vl1

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{{Seed}}
 
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[[Image:2vl1.png|left|200px]]
 
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==Crystal structure of beta-alanine synthase from Saccharomyces kluyveri in complex with a gly-gly peptide==
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The line below this paragraph, containing "STRUCTURE_2vl1", creates the "Structure Box" on the page.
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<StructureSection load='2vl1' size='340' side='right'caption='[[2vl1]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vl1]] 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=2VL1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VL1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2vl1| PDB=2vl1 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vl1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vl1 OCA], [https://pdbe.org/2vl1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vl1 RCSB], [https://www.ebi.ac.uk/pdbsum/2vl1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vl1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q96W94_LACKL Q96W94_LACKL]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vl/2vl1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2vl1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In nature, the same biochemical reaction can be catalyzed by enzymes having fundamentally different folds, reaction mechanisms and origins. For example, the third step of the reductive catabolism of pyrimidines, the conversion of N-carbamyl-beta-alanine to beta-alanine, is catalyzed by two beta-alanine synthase (beta ASase, EC 3.5.1.6) subfamilies. We show that the "prototype" eukaryote beta ASases, such as those from Drosophila melanogaster and Arabidopsis thaliana, are relatively efficient in the conversion of N-carbamyl-beta A compared with a representative of fungal beta ASases, the yeast Saccharomyces kluyveri beta ASase, which has a high K(m) value (71 mM). S. kluyveri beta ASase is specifically inhibited by dipeptides and tripeptides, and the apparent K(i) value of glycyl-glycine is in the same range as the substrate K(m). We show that this inhibitor binds to the enzyme active center in a similar way as the substrate. The observed structural similarities and inhibition behavior, as well as the phylogenetic relationship, suggest that the ancestor of the fungal beta ASase was a protease that had modified its profession and become involved in the metabolism of nucleic acid precursors.
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===CRYSTAL STRUCTURE OF BETA-ALANINE SYNTHASE FROM SACCHAROMYCES KLUYVERI IN COMPLEX WITH THE A GLY-GLY PEPTIDE===
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A recruited protease is involved in catabolism of pyrimidines.,Andersen B, Lundgren S, Dobritzsch D, Piskur J J Mol Biol. 2008 May 30;379(2):243-50. Epub 2008 Apr 7. PMID:18448119<ref>PMID:18448119</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_18448119}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2vl1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18448119 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18448119}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2VL1 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=2VL1 OCA].
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==Reference==
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A recruited protease is involved in catabolism of pyrimidines., Andersen B, Lundgren S, Dobritzsch D, Piskur J, J Mol Biol. 2008 May 30;379(2):243-50. Epub 2008 Apr 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18448119 18448119]
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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]
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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]
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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]
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[[Category: Beta-ureidopropionase]]
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[[Category: Lachancea kluyveri]]
[[Category: Lachancea kluyveri]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Andersen, B.]]
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[[Category: Andersen B]]
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[[Category: Dobritzsch, D.]]
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[[Category: Dobritzsch D]]
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[[Category: Lundgren, S.]]
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[[Category: Lundgren S]]
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[[Category: Piskur, J.]]
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[[Category: Piskur J]]
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[[Category: Alpha and beta protein]]
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[[Category: Amidohydrolase]]
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[[Category: Complex with glycine-glycine]]
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[[Category: Di-zinc center]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:15:47 2008''
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Current revision

Crystal structure of beta-alanine synthase from Saccharomyces kluyveri in complex with a gly-gly peptide

PDB ID 2vl1

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