2vlb

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{{Seed}}
 
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[[Image:2vlb.png|left|200px]]
 
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==Structure of unliganded arylmalonate decarboxylase==
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The line below this paragraph, containing "STRUCTURE_2vlb", creates the "Structure Box" on the page.
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<StructureSection load='2vlb' size='340' side='right'caption='[[2vlb]], [[Resolution|resolution]] 1.92&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'>[[2vlb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_bronchiseptica Bordetella bronchiseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VLB 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]] 1.92&#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=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_2vlb| PDB=2vlb | 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=2vlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vlb OCA], [https://pdbe.org/2vlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vlb RCSB], [https://www.ebi.ac.uk/pdbsum/2vlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vlb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMDA_BORBO AMDA_BORBO]
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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/2vlb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2vlb 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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Arylmalonate decarboxylase (AMDase) from Bordetella bronchiseptica catalyzes the enantioselective decarboxylation of arylmethylmalonates without the need for an organic cofactor or metal ion. The decarboxylation reaction is of interest for the synthesis of fine chemicals. As basis for an analysis of the catalytic mechanism of AMDase and for a rational enzyme design, we determined the X-ray structure of the enzyme up to 1.9 A resolution. Like the distantly related aspartate or glutamate racemases, AMDase has an aspartate transcarbamoylase fold consisting of two alpha/beta domains related by a pseudo dyad. However, the domain orientation of AMDase differs by about 30 degrees from that of the glutamate racemases, and also significant differences in active-site structures are observed. In the crystals, four independent subunits showing different conformations of active-site loops are present. This finding is likely to reflect the active-site mobility necessary for catalytic activity.
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===STRUCTURE OF UNLIGANDED ARYLMALONATE DECARBOXYLASE===
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Active-site mobility revealed by the crystal structure of arylmalonate decarboxylase from Bordetella bronchiseptica.,Kuettner EB, Keim A, Kircher M, Rosmus S, Strater N J Mol Biol. 2008 Mar 21;377(2):386-94. Epub 2008 Jan 5. PMID:18258259<ref>PMID:18258259</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_18258259}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2vlb" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18258259 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18258259}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2VLB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bordetella_bronchiseptica Bordetella bronchiseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VLB OCA].
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==Reference==
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Active-site mobility revealed by the crystal structure of arylmalonate decarboxylase from Bordetella bronchiseptica., Kuettner EB, Keim A, Kircher M, Rosmus S, Strater N, J Mol Biol. 2008 Mar 21;377(2):386-94. Epub 2008 Jan 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18258259 18258259]
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[[Category: Arylmalonate decarboxylase]]
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[[Category: Bordetella bronchiseptica]]
[[Category: Bordetella bronchiseptica]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Keim, A.]]
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[[Category: Keim A]]
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[[Category: Kircher, M.]]
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[[Category: Kircher M]]
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[[Category: Kuettner, E B.]]
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[[Category: Kuettner EB]]
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[[Category: Rosmus, S.]]
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[[Category: Rosmus S]]
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[[Category: Strater, N.]]
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[[Category: Strater N]]
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[[Category: Amdase]]
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[[Category: Decarboxylase]]
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[[Category: Decarboxylation]]
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[[Category: Lyase]]
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[[Category: Protein dynamic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:47:42 2008''
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Current revision

Structure of unliganded arylmalonate decarboxylase

PDB ID 2vlb

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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