1gao: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1gao.gif|left|200px]]
{{Seed}}
[[Image:1gao.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gao|  PDB=1gao  |  SCENE=  }}  
{{STRUCTURE_1gao|  PDB=1gao  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE L44S MUTANT OF FERREDOXIN I'''
===CRYSTAL STRUCTURE OF THE L44S MUTANT OF FERREDOXIN I===




==Overview==
<!--
The reduction potential (E(0)') of the [4Fe-4S](2+/+) cluster of Azotobacter vinelandii ferredoxin I (AvFdI) and related ferredoxins is approximately 200 mV more negative than the corresponding clusters of Peptostreptococcus asaccharolyticus ferredoxin and related ferredoxins. Previous studies have shown that these differences in E(0)' do not result from the presence or absence of negatively charged surface residues or in differences in the types of hydrophobic residues found close to the [4Fe-4S](2+/+) clusters. Recently, a third, quite distinct class of ferredoxins (represented by the structurally characterized Chromatium vinosum ferredoxin) was shown to have a [4Fe-4S](2+/+) cluster with a very negative E(0)' similar to that of AvFdI. The observation that the sequences and structures surrounding the very negative E(0)' clusters in quite dissimilar proteins were almost identical inspired the construction of three additional mutations in the region of the [4Fe-4S](2+/+) cluster of AvFdI. The three mutations, V19E, P47S, and L44S, that incorporated residues found in the higher E(0)' P. asaccharolyticus ferredoxin all led to increases in E(0)' for a total of 130 mV with a 94-mV increase in the case of L44S. The results are interpreted in terms of x-ray structures of the FdI variants and show that the major determinant for the large increase in L44S is the introduction of an OH-S bond between the introduced Ser side chain and the Sgamma atom of Cys ligand 42 and an accompanying movement of water.
The line below this paragraph, {{ABSTRACT_PUBMED_11704670}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11704670 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11704670}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Ferredoxin]]
[[Category: Ferredoxin]]
[[Category: Iron-sulfur cluster]]
[[Category: Iron-sulfur cluster]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:21:23 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:00:11 2008''

Revision as of 02:00, 1 July 2008

File:1gao.png

Template:STRUCTURE 1gao

CRYSTAL STRUCTURE OF THE L44S MUTANT OF FERREDOXIN I

Template:ABSTRACT PUBMED 11704670

About this Structure

1GAO is a Single protein structure of sequence from Azotobacter vinelandii. Full crystallographic information is available from OCA.

Reference

Azotobacter vinelandii ferredoxin I: a sequence and structure comparison approach to alteration of [4Fe-4S]2+/+ reduction potential., Chen K, Jung YS, Bonagura CA, Tilley GJ, Prasad GS, Sridhar V, Armstrong FA, Stout CD, Burgess BK, J Biol Chem. 2002 Feb 15;277(7):5603-10. Epub 2001 Nov 9. PMID:11704670

Page seeded by OCA on Tue Jul 1 05:00:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1gao&oldid=601356"