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| <StructureSection load='2dzd' size='340' side='right'caption='[[2dzd]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2dzd' size='340' side='right'caption='[[2dzd]], [[Resolution|resolution]] 2.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2dzd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_thermodenitrificans"_klaushofer_and_hollaus_1970 "bacillus thermodenitrificans" klaushofer and hollaus 1970]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DZD FirstGlance]. <br> | + | <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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dzd OCA], [http://pdbe.org/2dzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dzd RCSB], [http://www.ebi.ac.uk/pdbsum/2dzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dzd ProSAT]</span></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> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q05FZ3_GEOTD Q05FZ3_GEOTD] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </div> | | </div> |
| <div class="pdbe-citations 2dzd" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2dzd" style="background-color:#fffaf0;"></div> |
| + | |
| + | ==See Also== |
| + | *[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bacillus thermodenitrificans klaushofer and hollaus 1970]] | + | [[Category: Geobacillus thermodenitrificans]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Pyruvate carboxylase]]
| + | [[Category: Islam MN]] |
- | [[Category: Islam, M N]] | + | [[Category: Kondo H]] |
- | [[Category: Kondo, H]] | + | [[Category: Kondo S]] |
- | [[Category: Kondo, S]] | + | [[Category: Nakajima Y]] |
- | [[Category: Nakajima, Y]] | + | [[Category: Sueda S]] |
- | [[Category: Sueda, S]] | + | [[Category: Sugio S]] |
- | [[Category: Sugio, S]] | + | |
- | [[Category: Bacillus thermodenitrifican]]
| + | |
- | [[Category: Biotin carboxylase]]
| + | |
- | [[Category: Ligase]]
| + | |
| Structural highlights
Function
Q05FZ3_GEOTD
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kondo S, Nakajima Y, Sugio S, Sueda S, Islam MN, Kondo H. Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans. Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):885-90. Epub 2007, Jul 17. PMID:17642515 doi:10.1107/S0907444907029423
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