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Published online before print May 28, 2004, 10.1110/ps.04661904
Protein Science (2004), 13:1942-1947. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FOR THE RECORD

The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA

Savvas N. Savvides1, Srinivasan Raghunathan2, Klaus Fütterer3, Alex G. Kozlov, Timothy M. Lohman and Gabriel Waksman4

Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA

(RECEIVED January 29, 2004; FINAL REVISION March 31, 2004; ACCEPTED March 31, 2004)



Abstract

The crystal structure of full-length homotetrameric single-stranded DNA (ssDNA)-binding protein from Escherichia coli (SSB) has been determined to 3.3 Å resolution and reveals that the entire C-terminal domain is disordered even in the presence of ssDNA. To our knowledge, this is the first experimental evidence that the C-terminal domain of SSB may be inherently disordered. The N-terminal DNA-binding domain of the protein is well ordered and is virtually indistinguishable from the previously determined structure of the chymotryptic fragment of SSB (SSBc) in complex with ssDNA. The absence of observable interactions with the core protein and the crystal packing of SSB together suggest that the disordered C-terminal domains likely extend laterally away from the DNA- binding domains, which may facilitate interactions with components of the replication machinery in vivo. The structure also reveals the conservation of molecular contacts between successive tetramers mediated by the L45 loops as seen in two other crystal forms of SSBc, suggesting a possible functional relevance of this interaction.

Keywords: SSB; crystal structure; DNA replication; ssDNA, protein disorder

Reprint requests to: Gabriel Waksman, Institute of Structural Molecular Biology, University College and Birkbeck College, Malet Street, London WC1E 7HX, UK; e-mail: g.waksman{at}mail.cryst.bbk.ac.uk; fax: 44-0207-631-6833.

1 Present addresses: Department of Biochemistry, Physiology and Microbiology, Ghent University, 9000 Ghent, Belgium;

2 The University of Texas Southwestern Medical Center at Dallas, Dallas TX 75390, USA;

3 School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK;

4 Institute of Structural Molecular Biology, University College and Birkbeck College, London WC1E 7HX, UK.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04661904.


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