2qla: Difference between revisions

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caption="2qla, resolution 2.900Å" />
caption="2qla, resolution 2.900Å" />
'''Crystal Structure of a 16-Helix Bundle Architecture Produced by the Zinc-Mediated Self Assembly of Four Cytochrome cb562 Molecules'''<br />
'''Crystal Structure of a 16-Helix Bundle Architecture Produced by the Zinc-Mediated Self Assembly of Four Cytochrome cb562 Molecules'''<br />
==Overview==
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.


==About this Structure==
==About this Structure==
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]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn Binding Site For Residue A 500'>AC1</scene>, <scene name='pdbsite=AC2:Zn Binding Site For Residue C 501'>AC2</scene>, <scene name='pdbsite=AC3:Zn Binding Site For Residue B 502'>AC3</scene>, <scene name='pdbsite=AC4:Zn Binding Site For Residue D 503'>AC4</scene>, <scene name='pdbsite=AC5:Hem Binding Site For Residue A 150'>AC5</scene>, <scene name='pdbsite=AC6:Hem Binding Site For Residue B 151'>AC6</scene>, <scene name='pdbsite=AC7:Hem Binding Site For Residue C 152'>AC7</scene> and <scene name='pdbsite=AC8:Hem Binding Site For Residue D 153'>AC8</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QLA OCA].  
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]. Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+500'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+C+501'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+B+502'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+D+503'>AC4</scene>, <scene name='pdbsite=AC5:Hem+Binding+Site+For+Residue+A+150'>AC5</scene>, <scene name='pdbsite=AC6:Hem+Binding+Site+For+Residue+B+151'>AC6</scene>, <scene name='pdbsite=AC7:Hem+Binding+Site+For+Residue+C+152'>AC7</scene> and <scene name='pdbsite=AC8:Hem+Binding+Site+For+Residue+D+153'>AC8</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QLA OCA].  


==Reference==
==Reference==
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]
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: Single protein]]
[[Category: Faraone-Mennella, J.]]
[[Category: Faraone-Mennella, J.]]
[[Category: Salgado, E.N.]]
[[Category: Salgado, E N.]]
[[Category: Tezcan, F.A.]]
[[Category: Tezcan, F A.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: ZN]]
[[Category: ZN]]
Line 27: Line 24:
[[Category: transport]]
[[Category: transport]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:58:54 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:40:16 2008''

Revision as of 16:40, 21 February 2008

File:2qla.jpg


2qla, resolution 2.900Å

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

About this Structure

2QLA is a Single protein structure of sequence from Escherichia coli with ZN and HEM as ligands. Known structural/functional Sites: AC1, AC2, AC3, AC4, AC5, AC6, AC7 and AC8. Full crystallographic information is available from OCA.

Reference

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:17929927

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