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| - | [[Image:1bbh.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1bbh| PDB=1bbh | SCENE= }} | | {{STRUCTURE_1bbh| PDB=1bbh | SCENE= }} |
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| - | '''ATOMIC STRUCTURE OF A CYTOCHROME C' WITH AN UNUSUAL LIGAND-CONTROLLED DIMER DISSOCIATION AT 1.8 ANGSTROMS RESOLUTION'''
| + | ===ATOMIC STRUCTURE OF A CYTOCHROME C' WITH AN UNUSUAL LIGAND-CONTROLLED DIMER DISSOCIATION AT 1.8 ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | The crystallographic structure of cytochrome c' from the purple phototrophic bacterium Chromatium vinosum (CVCP) has been determined at 1.8 A resolution using multiple isomorphous replacement. The molecule is a dimer, with each 131-residue chain folding as a four-helical bundle incorporating a covalently bound heme group at the core. This structure is the third of the ubiquitous cytochromes c' to be solved and is similar to the known structures of cytochrome c' from R. molischianum (RMCP) and R. rubrum (RRCP). CVCP is unique in exhibiting ligand-controlled dimer dissociation while RMCP and RRCP do not. The Tyr16 side-chain, which replaced Met16 in RMCP and Leu14 in RRCP, is parallel to the heme plane and located directly above the sixth ligand site of the heme Fe. Any ligand binding to this site, such as CO or CN-, must move the Tyr16 side-chain, which would be expected to cause other conformational changes of helix A, which contributes to the dimer interface, and consequently disrupting the dimer. Thus, the crystallographic structure of CVCP suggests a mechanism for dimer dissociation upon ligand binding. The dimer interface specificity is due to a lock and key shape complementarity of hydrophobic residues and not to any charge complementarity or cross-interface hydrogen bonds as is common in other protein-protein interfaces. The co-ordinates have been deposited in the Brookhaven Data Bank (entry P1BBH). | + | The line below this paragraph, {{ABSTRACT_PUBMED_8230224}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8230224 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8230224}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mcree, D E.]] | | [[Category: Mcree, D E.]] |
| | [[Category: Ren, Z.]] | | [[Category: Ren, Z.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:18:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:45:58 2008'' |
Revision as of 15:46, 30 June 2008
Template:STRUCTURE 1bbh
ATOMIC STRUCTURE OF A CYTOCHROME C' WITH AN UNUSUAL LIGAND-CONTROLLED DIMER DISSOCIATION AT 1.8 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 8230224
About this Structure
1BBH is a Single protein structure of sequence from Allochromatium vinosum. Full crystallographic information is available from OCA.
Reference
Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 A resolution., Ren Z, Meyer T, McRee DE, J Mol Biol. 1993 Nov 20;234(2):433-45. PMID:8230224
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