1bbh
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1bbh |SIZE=350|CAPTION= <scene name='initialview01'>1bbh</scene>, resolution 1.8Å | |PDB= 1bbh |SIZE=350|CAPTION= <scene name='initialview01'>1bbh</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbh OCA], [http://www.ebi.ac.uk/pdbsum/1bbh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bbh RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Mcree, D E.]] | [[Category: Mcree, D E.]] | ||
[[Category: Ren, Z.]] | [[Category: Ren, Z.]] | ||
| - | [[Category: HEM]] | ||
[[Category: electron transport(heme protein)]] | [[Category: electron transport(heme protein)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:57:37 2008'' |
Revision as of 15:57, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ATOMIC STRUCTURE OF A CYTOCHROME C' WITH AN UNUSUAL LIGAND-CONTROLLED DIMER DISSOCIATION AT 1.8 ANGSTROMS RESOLUTION
Overview
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).
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
Page seeded by OCA on Sun Mar 30 18:57:37 2008
