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.


1hh5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hh5.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hh5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hh5| PDB=1hh5 | SCENE= }}
{{STRUCTURE_1hh5| PDB=1hh5 | SCENE= }}
-
'''CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS'''
+
===CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS===
-
==Overview==
+
<!--
-
Multihaem cytochromes play a key role in electron-transport reactions in the periplasm of sulfate- and sulfur-reducing bacteria. The redox proteins grouped in the c3 superfamily also display metal-reducing activities, which make them interesting biotechnological tools. The crystal structure of the fully oxidized cytochrome c7 from Desulfuromonas acetoxidans has been solved by combined molecular-replacement and MAD methods. The structure has been refined at 1.9 A resolution to an R value of 19.1% (R(free) = 24.3%) and includes three haems and 116 water molecules. The protein displays the cytochrome c3 fold in a highly minimized form, while haem 2 and the surrounding protein environment are missing. The geometry of haem packing and of the haem axial ligands and propionates are described and compared with that of c3 cytochromes. The crystal structure is compared with the solution structure recently obtained by NMR methods and with its homologue cytochromes of the c3 superfamily. Comparison of the high number of available structures makes it possible to analyze the structural role of the few highly conserved residues, in addition to the cysteines and histidines that link the porphyrin rings and the Fe atoms to the protein chain.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11320307}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11320307 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11320307}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Electron transport]]
[[Category: Electron transport]]
[[Category: Multiheme cytochrome]]
[[Category: Multiheme cytochrome]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:50:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:10:53 2008''

Revision as of 05:10, 1 July 2008

Image:1hh5.png

Template:STRUCTURE 1hh5

CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS

Template:ABSTRACT PUBMED 11320307

About this Structure

1HH5 is a Single protein structure of sequence from Desulfuromonas acetoxidans. Full crystallographic information is available from OCA.

Reference

Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 A resolution., Czjzek M, Arnoux P, Haser R, Shepard W, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):670-8. Epub 2001, Apr 24. PMID:11320307

Page seeded by OCA on Tue Jul 1 08:10:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hh5"
Personal tools