Andrade, Susana L. A. and Cruz, Francisco and Drennan, Catherine L. and Ramakrishnan, Vijay and Rees, Douglas C. and Ferry, James G. and Einsle, Oliver (2005) Structures of the Iron-Sulfur Flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidus. Journal of Bacteriology, 187 (11). pp. 3848-3854. ISSN 0021-9193. http://resolver.caltech.edu/CaltechAUTHORS:ANDjbact05
See Usage Policy.
Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:ANDjbact05
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.
|Additional Information:||Copyright © 2005, American Society for Microbiology Received 10 January 2005/ Accepted 21 February 2005 We thank Hsiu-Ju Chiu for her assistance with data analysis. This work was supported in part by a Marie Curie Intra-European Fellowship within FP6 (to S.L.A.A.), by NIH grants GM45162 (to D.C.R.) and F32-GM19044 (to C.L.D.), and by Department of Energy grant DE-FG02-95ER20198 (to J.G.F.). Stanford Synchrotron Radiation Laboratory operations are funded by the U.S. Department of Energy Office of Basic Energy Sciences and the NIH.|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Archive Administrator|
|Deposited On:||20 Feb 2006|
|Last Modified:||26 Dec 2012 08:46|
Repository Staff Only: item control page