Structures of the iron-sulfur flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidus.

Abstract:

:Iron-sulfur flavoproteins (ISF) constitute a widespread family of redox-active proteins in anaerobic prokaryotes. Based on sequence homologies, their overall structure is expected to be similar to that of flavodoxins, but in addition to a flavin mononucleotide cofactor they also contain a cubane-type [4Fe:4S] cluster. In order to gain further insight into the function and properties of ISF, the three-dimensional structures of two ISF homologs, one from the thermophilic methanogen Methanosarcina thermophila and one from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus, were determined. The structures indicate that ISF assembles to form a tetramer and that electron transfer between the two types of redox cofactors requires oligomerization to juxtapose the flavin mononucleotide and [4Fe:4S] cluster bound to different subunits. This is only possible between different monomers upon oligomerization. Fundamental differences in the surface properties of the two ISF homologs underscore the diversity encountered within this protein family.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Andrade SL,Cruz F,Drennan CL,Ramakrishnan V,Rees DC,Ferry JG,Einsle O

doi

10.1128/JB.187.11.3848-3854.2005

keywords:

subject

Has Abstract

pub_date

2005-06-01 00:00:00

pages

3848-54

issue

11

eissn

0021-9193

issn

1098-5530

pii

187/11/3848

journal_volume

187

pub_type

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