1ulz: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ulz.png|left|200px]]


{{STRUCTURE_1ulz| PDB=1ulz | SCENE= }}
==Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase==
<StructureSection load='1ulz' size='340' side='right'caption='[[1ulz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O67483_AQUAE O67483_AQUAE]
== 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/ul/1ulz_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=1ulz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===Crystal structure of the biotin carboxylase subunit of pyruvate carboxylase===
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>


{{ABSTRACT_PUBMED_14993673}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1ulz" style="background-color:#fffaf0;"></div>
[[1ulz]] is a 1 chain structure of [[Biotin carboxylase]] with 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].


==See Also==
==See Also==
*[[Biotin carboxylase|Biotin carboxylase]]
*[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:014993673</ref><references group="xtra"/>
__TOC__
[[Category: Aquifex aeolicus]]
</StructureSection>
[[Category: Pyruvate carboxylase]]
[[Category: Aquifex aeolicus VF5]]
[[Category: Kondo, H.]]
[[Category: Large Structures]]
[[Category: Kondo, S.]]
[[Category: Kondo H]]
[[Category: Nakajima, Y.]]
[[Category: Kondo S]]
[[Category: Sueda, S.]]
[[Category: Nakajima Y]]
[[Category: Sugio, S.]]
[[Category: Sueda S]]
[[Category: Yong-Biao, J.]]
[[Category: Sugio S]]
[[Category: Aquifex aeolicus]]
[[Category: Yong-Biao J]]
[[Category: Biotin carboxylase]]
[[Category: Ligase]]
[[Category: Pyruvate carboxylase]]
Retrieved from "https://proteopedia.org/1ulz"