Sandbox Reserved 335

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This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.

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spinqualitylabelsall models PDB ID 3cp5 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
3cp5, resolution 1.24Å ()
Ligands:	,
Gene:	cytC (Rhodothermus marinus)
Structural annotation: Resources: UniProt : B3FQS5
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

Cytochrome c (cyt c) is a superfamily of proteins belonging to the class of all-α proteins with a core of helices and a covalently-bound heme prosthetic group.^[1][2] The cytochrome c superfamily contains many different families including monodomain and multi-domain C-type cytochromes (ex. cyt c4, a two-domain C-type cytochrome, and NrfB, a pentaheme C-type cytochrome). This page focuses mainly on the cytochrome c superfamily, briefly discussing various types within the superfamily. The monoheme cytochrome c will be discussed in greater detail than other C-type cytochromes.

Contents 1 Introduction 2 Function 3 Structure 4 Mechanism 5 Importance 6 References

Introduction

Function

Structure

All members in the C-type cytochrome superfamily contain a heme prosthetic group that is covalently attached to the protein via two thioether bonds to cysteine residues.^[2] Most cytochromes c occur in a CXXCH motif, where a histidine residue is one of the two axial ligands of the heme iron. The other axial position may be left vacant or be occupied mostly by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.^[2]

Mechanism

Importance

References

1. ↑ SCOP http://scop.mrc-lmb.cam.ac.uk/scop-1.75/data/scop.b.b.i.b.html
2. ↑ ^{2.0 2.1 2.2} Stelter M, Melo AM, Pereira MM, Gomes CM, Hreggvidsson GO, Hjorleifsdottir S, Saraiva LM, Teixeira M, Archer M. A Novel Type of Monoheme Cytochrome c: Biochemical and Structural Characterization at 1.23 A Resolution of Rhodothermus marinus Cytochrome c. Biochemistry. 2008 Oct 15. PMID:18855424 doi:10.1021/bi800999g