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1frx

From Proteopedia

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{{STRUCTURE_1frx| PDB=1frx | SCENE= }}
{{STRUCTURE_1frx| PDB=1frx | SCENE= }}
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'''STRUCTURE AND PROPERTIES OF C20S FDI MUTANT'''
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===STRUCTURE AND PROPERTIES OF C20S FDI MUTANT===
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==Overview==
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The [4Fe-4S] cluster of Azotobacter vinelandii ferredoxin I receives three of its four ligands from a Cys-Xaa-Xaa-Cys-Xaa-Xaa-Cys sequence at positions 39-45 while the fourth ligand, Cys20, is provided by a distal portion of the sequence. Previously we reported that the site-directed mutation of Cys20 to Ala (C20A protein) resulted in the formation of a new [4Fe-4S] cluster that obtained its fourth ligand from Cys24, a free cysteine in the native structure. That ligand exchange required significant protein rearrangement. Here we report the conversion of Cys20 to Ser (C20S protein), which gives the protein the opportunity either to retain the native structure and use the Ser20 O gamma as a ligand or to rearrange and use Cys24. X-ray crystallography demonstrates that the cluster does not use the Ser20 O gamma as a ligand; rather it rearranges to use Cys24. In the C20S protein the [4Fe-4S] cluster has altered stability and redox properties relative to either C20A or the native protein.
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(as it appears on PubMed at http://www.pubmed.gov), where 7479727 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7479727}}
==About this Structure==
==About this Structure==
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[[Category: Stout, C D.]]
[[Category: Stout, C D.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:41:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:51:11 2008''

Revision as of 00:51, 1 July 2008

Image:1frx.png

Template:STRUCTURE 1frx

STRUCTURE AND PROPERTIES OF C20S FDI MUTANT

Template:ABSTRACT PUBMED 7479727

About this Structure

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

Reference

Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligation., Shen B, Jollie DR, Diller TC, Stout CD, Stephens PJ, Burgess BK, Proc Natl Acad Sci U S A. 1995 Oct 24;92(22):10064-8. PMID:7479727

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