The crystal structure of the leptospiral hypothetical protein LIC12922 reveals homology with the periplasmic chaperone SurA
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
20/10/2012
20/10/2012
2011
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Resumo |
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. FAPESP[CEPID/CBME 98/14138-2] Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) FAPESP[SMolBNet 00/10266-8] Synchrotron SOLEIL Synchrotron SOLEIL FAPESP Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) PDEE/CAPES Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) |
Identificador |
JOURNAL OF STRUCTURAL BIOLOGY, v.173, n.2, p.312-322, 2011 1047-8477 http://producao.usp.br/handle/BDPI/28656 10.1016/j.jsb.2010.10.009 |
Idioma(s) |
eng |
Publicador |
ACADEMIC PRESS INC ELSEVIER SCIENCE |
Relação |
Journal of Structural Biology |
Direitos |
restrictedAccess Copyright ACADEMIC PRESS INC ELSEVIER SCIENCE |
Palavras-Chave | #LIC12922 #Crystal structure #Parvulin domain #SurA homology #Chaperone #MULTIPLE SEQUENCE ALIGNMENTS #PROLYL-ISOMERASE ACTIVITY #OUTER-MEMBRANE PROTEINS #ESCHERICHIA-COLI #TRIGGER FACTOR #MOLECULAR CHAPERONE #PARVULIN-LIKE #DATABASE #RIBOSOME #DOMAIN #Biochemistry & Molecular Biology #Biophysics #Cell Biology |
Tipo |
article original article publishedVersion |