2v07

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2v07.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2v07.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2v07| PDB=2v07 | SCENE= }}
{{STRUCTURE_2v07| PDB=2v07 | SCENE= }}
-
'''STRUCTURE OF THE ARABIDOPSIS THALIANA CYTOCHROME C6A V52Q VARIANT'''
+
===STRUCTURE OF THE ARABIDOPSIS THALIANA CYTOCHROME C6A V52Q VARIANT===
-
==Overview==
+
<!--
-
Cytochrome c6A is a unique dithio-cytochrome of green algae and plants. It has a very similar core structure to that of bacterial and algal cytochromes c6 but is unable to fulfill the same function of transferring electrons from cytochrome f to photosystem I. A key feature is that its heme midpoint potential is more than 200 mV below that of cytochrome c6 despite having His and Met as axial heme-iron ligands. To identify the molecular origins of the difference in potential, the structure of cytochrome c6 from the cyanobacterium Phormidium laminosum has been determined by X-ray crystallography and compared with the known structure of cytochrome c6A. One salient difference of the heme pockets is that a highly conserved Gln (Q51) in cytochrome c6 is replaced by Val (V52) in c6A. Using protein film voltammetry, we found that swapping these residues raised the c6A potential by +109 mV and decreased that of c6 by almost the same extent, -100 mV. X-ray crystallography of the V52Q protein showed that the Gln residue adopts the same configuration relative to the heme as in cytochrome c6 and we propose that this stereochemistry destabilizes the oxidized form of the heme. Consequently, replacement of Gln by Val was probably a key step in the evolution of cytochrome c6A from cytochrome c6, inhibiting reduction by the cytochrome b6f complex and facilitating establishment of a new function.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17625855}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17625855 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17625855}}
==About this Structure==
==About this Structure==
Line 43: Line 47:
[[Category: Transit peptide]]
[[Category: Transit peptide]]
[[Category: Transport]]
[[Category: Transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:56:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:41:47 2008''

Revision as of 09:41, 29 July 2008

Image:2v07.png

Template:STRUCTURE 2v07

STRUCTURE OF THE ARABIDOPSIS THALIANA CYTOCHROME C6A V52Q VARIANT

Template:ABSTRACT PUBMED 17625855

About this Structure

2V07 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Modulation of heme redox potential in the cytochrome c6 family., Worrall JA, Schlarb-Ridley BG, Reda T, Marcaida MJ, Moorlen RJ, Wastl J, Hirst J, Bendall DS, Luisi BF, Howe CJ, J Am Chem Soc. 2007 Aug 1;129(30):9468-75. Epub 2007 Jul 11. PMID:17625855

Page seeded by OCA on Tue Jul 29 12:41:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v07"
Personal tools