3cyt
From Proteopedia
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|PDB= 3cyt |SIZE=350|CAPTION= <scene name='initialview01'>3cyt</scene>, resolution 1.8Å | |PDB= 3cyt |SIZE=350|CAPTION= <scene name='initialview01'>3cyt</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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=3cyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cyt OCA], [http://www.ebi.ac.uk/pdbsum/3cyt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3cyt RCSB]</span> | ||
}} | }} | ||
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[[Category: Thunnus alalunga]] | [[Category: Thunnus alalunga]] | ||
[[Category: Takano, T.]] | [[Category: Takano, T.]] | ||
| - | [[Category: ACE]] | ||
| - | [[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 Mon Mar 31 05:32:53 2008'' |
Revision as of 02:32, 31 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REDOX CONFORMATION CHANGES IN REFINED TUNA CYTOCHROME C
Overview
Tuna ferrocytochrome c and ferricytochrome c have been refined independently at high resolution (1.5 A and 1.8 A) to crystallographic residual errors of 17.3% and 20.8%, respectively. Small but significant conformational differences are seen surrounding a buried water molecule that is hydrogen bonded to Asn-52, Tyr-67, and Thr-78. In the oxidized state, this water molecule is 1.0 A closer to the heme and the heme has moved 0.15 A out of its heme crevice; both changes lead to a more polar microenvironment for the heme. Chemical modification studies, patterns of evolutionary conservatism, structural differences in bacterial cytochromes, and x-ray studies all agree that the "active site" for cytochrome c is bounded by lysines 8, 13,27, 72, 79, 86, and 87 (thus containing the evolutionary conservative 72-87 loop) and has the buried water molecule just below its surface and the opening of the heme crevice slightly to one side.
About this Structure
3CYT is a Single protein structure of sequence from Thunnus alalunga. This structure supersedes the now removed PDB entry 1CYT. The following pages contain interesting information on the relation of 3CYT with [Aconitase and Iron Regulatory Protein 1]. Full crystallographic information is available from OCA.
Reference
Redox conformation changes in refined tuna cytochrome c., Takano T, Dickerson RE, Proc Natl Acad Sci U S A. 1980 Nov;77(11):6371-5. PMID:6256733
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