This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1m1r

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1m1r.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1m1r.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m1r| PDB=1m1r | SCENE= }}
{{STRUCTURE_1m1r| PDB=1m1r | SCENE= }}
-
'''Reduced p222 crystal structure of the tetraheme cytochrome c of Shewanella oneidensis MR1'''
+
===Reduced p222 crystal structure of the tetraheme cytochrome c of Shewanella oneidensis MR1===
-
==Overview==
+
<!--
-
The genus Shewanella produces a unique small tetraheme cytochrome c that is implicated in the iron oxide respiration pathway. It is similar in heme content and redox potential to the well known cytochromes c(3) but related in structure to the cytochrome c domain of soluble fumarate reductases from Shewanella sp. We report the crystal structure of the small tetraheme cytochrome c from Shewanella oneidensis MR-1 in two crystal forms and two redox states. The overall fold and heme core are surprisingly different from the soluble fumarate reductase structures. The high resolution obtained for an oxidized orthorhombic crystal (0.97 A) revealed several flexible regions. Comparison of the six monomers in the oxidized monoclinic space group (1.55 A) indicates flexibility in the C-terminal region containing heme IV. The reduced orthorhombic crystal structure (1.02 A) revealed subtle differences in the position of several residues, resulting in decreased solvent accessibility of hemes and the withdrawal of a positive charge from the molecular surface. The packing between monomers indicates that intermolecular electron transfer between any heme pair is possible. This suggests there is no unique site of electron transfer on the surface of the protein and that electron transfer partners may interact with any of the hemes, a process termed "electron-harvesting." This optimizes the efficiency of intermolecular electron transfer by maximizing chances of productive collision with redox partners.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12080059}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12080059 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12080059}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Atomic resolution]]
[[Category: Atomic resolution]]
[[Category: Reduced structure]]
[[Category: Reduced structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:31:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:01:58 2008''

Revision as of 20:02, 2 July 2008

Image:1m1r.png

Template:STRUCTURE 1m1r

Reduced p222 crystal structure of the tetraheme cytochrome c of Shewanella oneidensis MR1

Template:ABSTRACT PUBMED 12080059

About this Structure

1M1R is a Single protein structure of sequence from Shewanella oneidensis. Full crystallographic information is available from OCA.

Reference

Crystal structures at atomic resolution reveal the novel concept of "electron-harvesting" as a role for the small tetraheme cytochrome c., Leys D, Meyer TE, Tsapin AS, Nealson KH, Cusanovich MA, Van Beeumen JJ, J Biol Chem. 2002 Sep 20;277(38):35703-11. Epub 2002 Jun 21. PMID:12080059

Page seeded by OCA on Wed Jul 2 23:01:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m1r"
Personal tools