HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 32, 23194-23204, August 10, 2007

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 282/32/23194    most recent M701602200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sauvé, V. Articles by Hemmings, A. M. Search for Related Content PubMed PubMed Citation Articles by Sauvé, V. Articles by Hemmings, A. M. Social Bookmarking                      What's this?

The SoxYZ Complex Carries Sulfur Cycle Intermediates on a Peptide Swinging Arm^*

Véronique Sauvé, Stefano Bruno¹, Ben C. Berks², and Andrew M. Hemmings^¶3

From the Department of Biochemistry, University of Oxford, Oxford OX1 3QU and the School of Biological Sciences and ^¶School of Chemical Sciences and Pharmacy, University of East Anglia, Norwich NR4 7TJ, United Kingdom

The bacterial Sox (sulfur oxidizing) system allows the utilization of inorganic sulfur compounds in energy metabolism. Central to this process is the SoxYZ complex that carries the pathway intermediates on a cysteine residue near the C terminus of SoxY. Crystal structures have been determined for Paracoccus pantotrophus SoxYZ with the carrier cysteine in the underivatized state, conjugated to the polysulfide mimic -mercaptoethanol, and as the sulfonate adduct pathway intermediate. The carrier cysteine is located on a peptide swinging arm and is bracketed on either side by diglycine dipeptides acting as molecular universal joints. This structure provides a novel solution to the requirement that the cysteine-bound intermediates be able to access and orient themselves within the active sites of multiple partner enzymes. Adjacent to the swinging arm there is a conserved, deep, apolar pocket into which the -mercaptoethanol adduct extends. This pocket would be well suited to a role in protecting labile pathway intermediates from adventitious reactions.

Received for publication, February 23, 2007 , and in revised form, May 2, 2007.

^* This work was supported by the Biotechnology and Biological Sciences Research Council Grants P15195 [GenBank] and B15211. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental "Experimental Procedures," Tables S1 and S2, and Figs. S1–S6.

The atomic coordinates and structure factors (code 2OX5, 2OXG, and 2OXH) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

¹ Present address: Dipartimento di Biochimica e Biologia Molecolare, Facoltà di Farmacia, Parco Area delle Scienze 23/A, 43100 Parma, Italy.

² To whom correspondence may be addressed. Tel.: +44-1865-275250; Fax: +44-1865-275259; E-mail: ben.berks{at}bioch.ox.ac.uk. ³ To whom correspondence may be addressed. Tel.: +44-1603-592259; Fax: +44-1603-592250; E-mail: a.hemmings{at}uea.ac.uk.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				T. F. Oliveira, C. Vonrhein, P. M. Matias, S. S. Venceslau, I. A. C. Pereira, and M. Archer The Crystal Structure of Desulfovibrio vulgaris Dissimilatory Sulfite Reductase Bound to DsrC Provides Novel Insights into the Mechanism of Sulfate Respiration J. Biol. Chem., December 5, 2008; 283(49): 34141 - 34149. [Abstract] [Full Text] [PDF]

				T. Ogawa, T. Furusawa, R. Nomura, D. Seo, N. Hosoya-Matsuda, H. Sakurai, and K. Inoue SoxAX Binding Protein, a Novel Component of the Thiosulfate-Oxidizing Multienzyme System in the Green Sulfur Bacterium Chlorobium tepidum J. Bacteriol., September 15, 2008; 190(18): 6097 - 6110. [Abstract] [Full Text] [PDF]

				U. Kappler, P. V. Bernhardt, J. Kilmartin, M. J. Riley, J. Teschner, K. J. McKenzie, and G. R. Hanson SoxAX Cytochromes, a New Type of Heme Copper Protein Involved in Bacterial Energy Generation from Sulfur Compounds J. Biol. Chem., August 8, 2008; 283(32): 22206 - 22214. [Abstract] [Full Text] [PDF]

				D. Rother, J. Ringk, and C. G. Friedrich Sulfur oxidation of Paracoccus pantotrophus: the sulfur-binding protein SoxYZ is the target of the periplasmic thiol-disulfide oxidoreductase SoxS Microbiology, July 1, 2008; 154(7): 1980 - 1988. [Abstract] [Full Text] [PDF]