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.


1blu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1blu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1blu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1blu| PDB=1blu | SCENE= }}
{{STRUCTURE_1blu| PDB=1blu | SCENE= }}
-
'''STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CHROMATIUM VINOSUM'''
+
===STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CHROMATIUM VINOSUM===
-
==Overview==
+
<!--
-
The crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum has been solved by molecular replacement using data recorded with synchrotron radiation. The crystals were hexagonal prisms that showed a strong tendency to develop into long tubes. The hexagonal prisms diffracted to 2.1 A resolution at best, and a structural model for C. vinosum ferredoxin has been built with a final R of 19.2%. The N-terminal domain coordinates the two [4Fe-4S] clusters in a fold that is almost identical to that of other known ferredoxins. However, the structure has two unique features. One is a six-residue insertion between two ligands of one cluster forming a two-turn external loop; this short loop changes the conformation of the Cys 40 ligand compared to other ferredoxins and hampers the building of one NH...S H-bond to one of the inorganic sulfurs. The other remarkable structural element is a 3.5-turn alpha-helix at the C-terminus that covers one side of the same cluster and is linked to the cluster-binding domain by a six-residue external chain segment. The charge distribution is highly asymmetric over the molecule. The structure of C. vinosum ferredoxin strongly suggests divergent evolution for bacterial [3/4Fe-4S] ferredoxins from a common ancestral cluster-binding core. The unexpected slow intramolecular electron transfer rate between the clusters in C. vinosum ferredoxin, compared to other similar proteins, may be attributed to the unusual electronic properties of one of the clusters arising from localized changes in its vicinity rather than to a global structural rearrangement.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8880900}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8880900 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8880900}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Electron transport]]
[[Category: Electron transport]]
[[Category: Ferredoxin]]
[[Category: Ferredoxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:40:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:21:39 2008''

Revision as of 16:21, 30 June 2008

Image:1blu.png

Template:STRUCTURE 1blu

STRUCTURE OF THE 2[4FE-4S] FERREDOXIN FROM CHROMATIUM VINOSUM

Template:ABSTRACT PUBMED 8880900

About this Structure

1BLU is a Single protein structure of sequence from Allochromatium vinosum. Full crystallographic information is available from OCA.

Reference

Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins., Moulis JM, Sieker LC, Wilson KS, Dauter Z, Protein Sci. 1996 Sep;5(9):1765-75. PMID:8880900

Page seeded by OCA on Mon Jun 30 19:21:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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