3cyt

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[[Image:3cyt.gif|left|200px]]
[[Image:3cyt.gif|left|200px]]
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{{Structure
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{{STRUCTURE_3cyt| PDB=3cyt | SCENE= }}
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|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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'''REDOX CONFORMATION CHANGES IN REFINED TUNA CYTOCHROME C'''
'''REDOX CONFORMATION CHANGES IN REFINED TUNA CYTOCHROME C'''
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==About this Structure==
==About this Structure==
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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].
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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 [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cyt 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==
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[[Category: Thunnus alalunga]]
[[Category: Thunnus alalunga]]
[[Category: Takano, T.]]
[[Category: Takano, T.]]
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[[Category: electron transport (heme protein)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:59:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:32:53 2008''
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Revision as of 18:59, 4 May 2008

Template:STRUCTURE 3cyt

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 Sun May 4 21:59:52 2008

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