2qla: Difference between revisions

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New page: left|200px<br /><applet load="2qla" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qla, resolution 2.900Å" /> '''Crystal Structure o...
 
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[[Image:2qla.jpg|left|200px]]<br /><applet load="2qla" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2qla, resolution 2.900&Aring;" />
'''Crystal Structure of a 16-Helix Bundle Architecture Produced by the Zinc-Mediated Self Assembly of Four Cytochrome cb562 Molecules'''<br />


==Overview==
==Crystal Structure of a 16-Helix Bundle Architecture Produced by the Zinc-Mediated Self Assembly of Four Cytochrome cb562 Molecules==
The prediction, design, and control of protein-protein interactions (PPIs), remain great challenges despite recent advances. Here we describe the, chemical control of PPIs through the use of metal coordination, which, circumvents the requirement of PPIs for an extensive set of weak, interactions spread over a large surface. A non-self-associating, four-bundle protein, cytochrome cb562, with appropriately engineered, metal-binding motifs self-assembles to a 16-helix quaternary structure, upon addition of equimolar Zn. The crystal structure of the assembly, combined with PFG diffusion NMR and sedimentation velocity experiments, indicates that the oligomerization properties of cytochrome cb562 are, governed entirely by metal coordination without significant thermodynamic, bias from specific PPIs.
<StructureSection load='2qla' size='340' side='right'caption='[[2qla]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2qla]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QLA 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2qla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qla OCA], [https://pdbe.org/2qla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qla RCSB], [https://www.ebi.ac.uk/pdbsum/2qla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qla ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.
== 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/ql/2qla_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=2qla ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2QLA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QLA OCA].
*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Controlling Protein-Protein Interactions through Metal Coordination: Assembly of a 16-Helix Bundle Protein., Salgado EN, Faraone-Mennella J, Tezcan FA, J Am Chem Soc. 2007 Nov 7;129(44):13374-5. Epub 2007 Oct 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17929927 17929927]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Faraone-Mennella, J.]]
[[Category: Faraone-Mennella J]]
[[Category: Salgado, E.N.]]
[[Category: Salgado EN]]
[[Category: Tezcan, F.A.]]
[[Category: Tezcan FA]]
[[Category: HEM]]
[[Category: ZN]]
[[Category: 16-helix bundle]]
[[Category: electron transport]]
[[Category: heme]]
[[Category: interfacial zn-coordination]]
[[Category: iron]]
[[Category: metal-binding]]
[[Category: periplasm]]
[[Category: transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:23:35 2008''

Latest revision as of 14:35, 30 August 2023

Crystal Structure of a 16-Helix Bundle Architecture Produced by the Zinc-Mediated Self Assembly of Four Cytochrome cb562 MoleculesCrystal Structure of a 16-Helix Bundle Architecture Produced by the Zinc-Mediated Self Assembly of Four Cytochrome cb562 Molecules

Structural highlights

2qla is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C562_ECOLX Electron-transport protein of unknown function.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2qla, resolution 2.90Å

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