View source for 2dzd


==Crystal structure of the biotin carboxylase domain of pyruvate carboxylase==
<StructureSection load='2dzd' size='340' side='right'caption='[[2dzd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dzd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DZD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=2dzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dzd OCA], [https://pdbe.org/2dzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dzd RCSB], [https://www.ebi.ac.uk/pdbsum/2dzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dzd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q05FZ3_GEOTD Q05FZ3_GEOTD] 
== 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/dz/2dzd_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=2dzd ConSurf].
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== Publication Abstract from PubMed ==
The biotin carboxylase (BC) domain of pyruvate carboxylase (PC) from Bacillus thermodenitrificans (BC-bPC) was crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6, b = 116.0, c = 115.7 A. Two BC protomers are contained in the asymmetric unit. Diffraction data were collected at 100 K and the crystal structure was solved by the molecular-replacement method and refined against reflections in the 20.0-2.4 A resolution range, giving an R factor of 0.235 and a free R factor of 0.292. The overall structure of BC-bPC is similar to those of the BC subunits of Aquifex aeolicus PC (BC-aPC) and Escherichia coli ACC (BC-eACC). The crystal structure revealed that BC-bPC forms a unique dimeric quaternary structure, which might be caused as a result of the division of the BC domain from the rest of the protein. The position of domain B in BC-bPC differs from those in other enzymes of similar structure (BC-aPC and BC-eACC).

Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans.,Kondo S, Nakajima Y, Sugio S, Sueda S, Islam MN, Kondo H Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):885-90. Epub 2007, Jul 17. PMID:17642515<ref>PMID:17642515</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2dzd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus thermodenitrificans]]
[[Category: Large Structures]]
[[Category: Islam MN]]
[[Category: Kondo H]]
[[Category: Kondo S]]
[[Category: Nakajima Y]]
[[Category: Sueda S]]
[[Category: Sugio S]]