The crystal structure of the leptospiral hypotheti... - BV FAPESP
Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The crystal structure of the leptospiral hypothetical protein LIC12922 reveals homology with the periplasmic chaperone SurA

Full text
Author(s):
Giuseppe, Priscila O. [1] ; Von Atzingen, Marina [2] ; Nascimento, Ana Lucia T. O. [3, 2] ; Zanchin, Nilson I. T. [4] ; Guimaraes, Beatriz G. [5]
Total Authors: 5
Affiliation:
[1] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Biosci Natl Lab LNBio, BR-13083970 Campinas, SP - Brazil
[2] Ctr Biotecnol, Inst Butantan, BR-05503900 Sao Paulo - Brazil
[3] Univ Sao Paulo, Inst Ciencias Biomed, Interunidades Biotecnol, BR-05508900 Sao Paulo - Brazil
[4] Univ Estadual Campinas, Ctr Biol Mol & Engn Genet, BR-13083875 Campinas, SP - Brazil
[5] LOrme Merisiers, Synchrotron SOLEIL, F-91192 Gif Sur Yvette - France
Total Affiliations: 5
Document type: Journal article
Source: Journal of Structural Biology; v. 173, n. 2, p. 312-322, FEB 2011.
Web of Science Citations: 6
Abstract

Leptospirosis is a world spread zoonosis caused by members of the genus Leptospira. Although leptospires were identified as the causal agent of leptospirosis almost 100 years ago, little is known about their biology, which hinders the development of new treatment and prevention strategies. One of the several aspects of the leptospiral biology not yet elucidated is the process by which outer membrane proteins (OMPs) traverse the periplasm and are inserted into the outer membrane. The crystal structure determination of the conserved hypothetical protein LIC12922 from Leptospira interrogans revealed a two domain protein homologous to the Escherichia coli periplasmic chaperone SurA. The LIC12922 NC-domain is structurally related to the chaperone modules of E. coli SurA and trigger factor, whereas the parvulin domain is devoid of peptidyl prolyl cis-trans isomerase activity. Phylogenetic analyses suggest a relationship between LIC12922 and the chaperones PrsA, PpiD and SurA. Based on our structural and evolutionary analyses, we postulate that LIC12922 is a periplasmic chaperone involved in OMPs biogenesis in Leptospira spp. Since LIC12922 homologs were identified in all spirochetal genomes sequenced to date, this assumption may have implications for the OMPs biogenesis studies not only in leptospires but in the entire Phylum Spirochaetes. (C) 2010 Elsevier Inc. All rights reserved. (AU)

FAPESP's process: 00/10266-8 - A structural biology laboratory network for the study of the 3D structures of proteins
Grantee:Nilson Ivo Tonin Zanchin
Support Opportunities: Genome Research Grants
FAPESP's process: 98/14138-2 - Center for Structural Molecular Biotechnology
Grantee:Glaucius Oliva
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC