1cyc

From Proteopedia

(Difference between revisions)

Revision as of 23:35, 10 September 2015

THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION

Structural highlights

1cyc is a 2 chain structure with sequence from Bonito. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CYC_KATPE] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure analysis of bonito heart ferrocytochrome c was carried out at 2.3 A resolution by X-ray diffraction, and a Kendrew-type skeletal model was built up. This molecule has an overall egg shape, 35 A in height, 30 A in width and 23 A in thickness; the 5th ligand of the heme iron atom is the N-epsilon atom of the His-18 imidazole ring and the 6th is the Met-80 sulfur atom. Distinct alpha-helix regions are found between the N-terminus and reside 11, between 60 and 69, and between 90 and the C-terminus. The most distinct difference between the conformation of the present molecule and that of the horse oxidized molecule is the location of the Phe-82 phenyl ring. In the present reduced molecule, the phyenyl ring is in closer contact with the iron atom and gives influences on the character of the iron atom. Inside the molecule, at the lower part of the heme pocket, there is an extended hydrogen bond network including the propionic acid residues of the heme group. Both Phe-82 and the hydrogen bond network may play a key role in the function of this molecule.

The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function.,Tanaka N, Yamane T, Tsukihara T, Ashida T, Kakudo M J Biochem. 1975 Jan 1;77(1?):147-62. PMID:166072^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tanaka N, Yamane T, Tsukihara T, Ashida T, Kakudo M. The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function. J Biochem. 1975 Jan 1;77(1?):147-62. PMID:166072

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://proteopedia.org/wiki/index.php/1cyc"

@@ Line 2: / Line 2: @@
 <StructureSection load='1cyc' size='340' side='right' caption='[[1cyc]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cyc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Katsuwonus_pelamis Katsuwonus pelamis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CYC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cyc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bonito Bonito]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CYC FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cyc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cyc RCSB], [http://www.ebi.ac.uk/pdbsum/1cyc PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cyc OCA], [http://pdbe.org/1cyc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cyc RCSB], [http://www.ebi.ac.uk/pdbsum/1cyc PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1cyc" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Katsuwonus pelamis]]
+[[Category: Bonito]]
 [[Category: Ashida, T]]
 [[Category: Kakudo, M]]

1cyc

From Proteopedia

Revision as of 23:35, 10 September 2015

THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox