3NRK
The crystal structure of the leptospiral hypothetical protein LIC12922
Summary for 3NRK
| Entry DOI | 10.2210/pdb3nrk/pdb |
| Descriptor | LIC12922 (1 entity in total) |
| Functional Keywords | nc domain, parvulin domain, sura homology, probable chaperone, unknown function |
| Biological source | Leptospira interrogans serovar Copenhageni |
| Total number of polymer chains | 1 |
| Total formula weight | 37840.01 |
| Authors | Giuseppe, P.O.,Atzingen, M.V.,Nascimento, A.L.T.O.,Zanchin, N.I.T.,Guimaraes, B.G. (deposition date: 2010-06-30, release date: 2010-11-24, Last modification date: 2023-12-27) |
| Primary citation | Giuseppe, P.O.,Von Atzingen, M.,Nascimento, A.L.,Zanchin, N.I.,Guimaraes, B.G. The crystal structure of the leptospiral hypothetical protein LIC12922 reveals homology with the periplasmic chaperone SurA. J.Struct.Biol., 173:312-322, 2011 Cited by PubMed 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. PubMed: 20970503DOI: 10.1016/j.jsb.2010.10.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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