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High Resolution Crystal Structures of the Wild Type and Cys-55 right-arrow Ser and Cys-59 right-arrow Ser Variants of the Thioredoxin-like [2Fe-2S] Ferredoxin from Aquifex aeolicus

Yeh, Andrew P. and Ambroggio, Xavier I. and Andrade, Susana L. A. and Einsle, Oliver and Chatelet, Claire and Meyer, Jacques and Rees, Douglas C. (2002) High Resolution Crystal Structures of the Wild Type and Cys-55 right-arrow Ser and Cys-59 right-arrow Ser Variants of the Thioredoxin-like [2Fe-2S] Ferredoxin from Aquifex aeolicus. Journal of Biological Chemistry, 277 (37). pp. 34499-34507. ISSN 0021-9258. https://resolver.caltech.edu/CaltechAUTHORS:YEHjbc02

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Abstract

The [2Fe-2S] ferredoxin (Fd4) from Aquifex aeolicus adopts a thioredoxin-like polypeptide fold that is distinct from other [2Fe-2S] ferredoxins. Crystal structures of the Cys-55 right-arrow Ser (C55S) and Cys-59 right-arrow Ser (C59S) variants of this protein have been determined to 1.25 Å and 1.05 Å resolution, respectively, whereas the resolution of the wild type (WT) has been extended to 1.5 Å. The improved WT structure provides a detailed description of the [2Fe-2S] cluster, including two features that have not been noted previously in any [2Fe-2S] cluster-containing protein, namely, pronounced distortions in the cysteine coordination to the cluster and a Calpha -H-Sgamma hydrogen bond between cluster ligands Cys-55 and Cys-9. These features may contribute to the unusual electronic and magnetic properties of the [2Fe-2S] clusters in WT and variants of this ferredoxin. The structures of the two variants of Fd4, in which single cysteine ligands to the [2Fe-2S] cluster are replaced by serine, establish the metric details of serine-ligated Fe-S active sites with unprecedented accuracy. Both the cluster and its surrounding protein matrix change in subtle ways to accommodate this ligand substitution, particularly in terms of distortions of the Fe2S2 inorganic core from planarity and displacements of the polypeptide chain. These high resolution structures illustrate how the interactions between polypeptide chains and Fe-S active sites reflect combinations of flexibility and rigidity on the part of both partners; these themes are also evident in more complex systems, as exemplified by changes associated with serine ligation of the nitrogenase P cluster.


Item Type:Article
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https://doi.org/10.1074/jbc.M205096200DOIUNSPECIFIED
ORCID:
AuthorORCID
Rees, Douglas C.0000-0003-4073-1185
Additional Information:Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc. Received for publication, May 23, 2002, and in revised form, June 25, 2002. Originally published In Press as doi:10.1074/jbc.M205096200 on June 27, 2002 Portions of this research were carried out at the Stanford Synchrotron Radiation Laboratory, a national user facility operated by Stanford University on behalf of the United States Department of Energy, Office of Basic Energy Sciences. The Stanford Synchrotron Radiation Laboratory Structural Molecular Biology Program is supported by the Department of Energy and the National Institutes of Health. This work was supported by National Institutes of Health Grant GM45062 (to D.C.R.) and by a predoctoral fellowship from the National Science Foundation (to X.I.A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. The atomic coordinates and the structure factors (code 1M2A, 1M2B and 1M2D) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
Issue or Number:37
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Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:YEHjbc02
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ID Code:5472
Collection:CaltechAUTHORS
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Deposited On:19 Oct 2006
Last Modified:02 Oct 2019 23:23

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