1ulz

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[[Image:1ulz.gif|left|200px]]
 
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==Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase==
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The line below this paragraph, containing "STRUCTURE_1ulz", creates the "Structure Box" on the page.
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<StructureSection load='1ulz' size='340' side='right'caption='[[1ulz]], [[Resolution|resolution]] 2.20&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'>[[1ulz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULZ 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]] 2.2&#8491;</td></tr>
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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=1ulz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ulz OCA], [https://pdbe.org/1ulz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ulz RCSB], [https://www.ebi.ac.uk/pdbsum/1ulz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ulz ProSAT]</span></td></tr>
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{{STRUCTURE_1ulz| PDB=1ulz | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O67483_AQUAE O67483_AQUAE]
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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/ul/1ulz_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=1ulz 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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Pyruvate carboxylase (PC) is distributed in many eukaryotes as well as in some prokaryotes. PC catalyzes the ATP-dependent carboxylation of pyruvate to form oxalacetate. PC has three functional domains, one of which is a biotin carboxylase (BC) domain. The BC subunit of PC from Aquifex aeolicus (PC-beta) was crystallized in an orthorhombic form with space group P2(1)2(1)2, unit-cell parameters a = 92.4, b = 122.1, c = 59.0 A and one molecule in the asymmetric unit. Diffraction data were collected at 100 K on BL24XU at SPring-8. The crystal structure was determined by the molecular-replacement method and refined against 20.0-2.2 A resolution data, giving an R factor of 0.199 and a free R factor of 0.236. The crystal structure revealed that PC-beta forms a dimeric quaternary structure consisting of two molecules related by crystallographic twofold symmetry. The overall structure of PC-beta is similar to other biotin-dependent carboxylases, such as acetyl-CoA carboxylase (ACC). Although some parts of domain B were disordered in ACC, the corresponding parts of PC-beta were clearly determined in the crystal structure. From comparison between the active-site structure of ACC with ATP bound and a virtual model of PC-beta with ATP bound, it was shown that the backbone torsion angles of Glu203 in PC-beta change and some of water molecules in the active site of PC-beta are excluded upon ATP binding.
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'''Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase'''
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Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution.,Kondo S, Nakajima Y, Sugio S, Yong-Biao J, Sueda S, Kondo H Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):486-92. Epub 2004, Feb 25. PMID:14993673<ref>PMID:14993673</ref>
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==Overview==
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Pyruvate carboxylase (PC) is distributed in many eukaryotes as well as in some prokaryotes. PC catalyzes the ATP-dependent carboxylation of pyruvate to form oxalacetate. PC has three functional domains, one of which is a biotin carboxylase (BC) domain. The BC subunit of PC from Aquifex aeolicus (PC-beta) was crystallized in an orthorhombic form with space group P2(1)2(1)2, unit-cell parameters a = 92.4, b = 122.1, c = 59.0 A and one molecule in the asymmetric unit. Diffraction data were collected at 100 K on BL24XU at SPring-8. The crystal structure was determined by the molecular-replacement method and refined against 20.0-2.2 A resolution data, giving an R factor of 0.199 and a free R factor of 0.236. The crystal structure revealed that PC-beta forms a dimeric quaternary structure consisting of two molecules related by crystallographic twofold symmetry. The overall structure of PC-beta is similar to other biotin-dependent carboxylases, such as acetyl-CoA carboxylase (ACC). Although some parts of domain B were disordered in ACC, the corresponding parts of PC-beta were clearly determined in the crystal structure. From comparison between the active-site structure of ACC with ATP bound and a virtual model of PC-beta with ATP bound, it was shown that the backbone torsion angles of Glu203 in PC-beta change and some of water molecules in the active site of PC-beta are excluded upon ATP binding.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1ULZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULZ OCA].
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</div>
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<div class="pdbe-citations 1ulz" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution., Kondo S, Nakajima Y, Sugio S, Yong-Biao J, Sueda S, Kondo H, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):486-92. Epub 2004, Feb 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14993673 14993673]
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*[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]]
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[[Category: Aquifex aeolicus]]
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== References ==
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[[Category: Pyruvate carboxylase]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Kondo, H.]]
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</StructureSection>
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[[Category: Kondo, S.]]
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[[Category: Aquifex aeolicus VF5]]
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[[Category: Nakajima, Y.]]
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[[Category: Large Structures]]
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[[Category: Sueda, S.]]
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[[Category: Kondo H]]
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[[Category: Sugio, S.]]
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[[Category: Kondo S]]
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[[Category: Yong-Biao, J.]]
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[[Category: Nakajima Y]]
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[[Category: Aquifex aeolicus]]
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[[Category: Sueda S]]
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[[Category: Biotin carboxylase]]
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[[Category: Sugio S]]
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[[Category: Pyruvate carboxylase]]
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[[Category: Yong-Biao J]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:24:39 2008''
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Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase

PDB ID 1ulz

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