3cyt
From Proteopedia
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| - | [[Image:3cyt.gif|left|200px]] | + | [[Image:3cyt.gif|left|200px]] |
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| - | '''REDOX CONFORMATION CHANGES IN REFINED TUNA CYTOCHROME C''' | + | {{Structure |
| + | |PDB= 3cyt |SIZE=350|CAPTION= <scene name='initialview01'>3cyt</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''REDOX CONFORMATION CHANGES IN REFINED TUNA CYTOCHROME C''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3CYT is a [ | + | 3CYT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thunnus_alalunga Thunnus alalunga]. This structure supersedes the now removed PDB entry 1CYT. The following pages contain interesting information on the relation of 3CYT with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb89_1.html Aconitase and Iron Regulatory Protein 1]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CYT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/6256733 6256733] |
[[Category: Aconitase and Iron Regulatory Protein 1]] | [[Category: Aconitase and Iron Regulatory Protein 1]] | ||
[[Category: Cytochrome c]] | [[Category: Cytochrome c]] | ||
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[[Category: electron transport (heme protein)]] | [[Category: electron transport (heme protein)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:04:25 2008'' |
Revision as of 17:04, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | and | ||||||
| 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
Page seeded by OCA on Thu Mar 20 19:04:25 2008
