2ZZ8

Crystal structure of LipL32, the most abundant surface protein of pathogenic leptospira spp

Summary for 2ZZ8

• Entry DOI: 10.2210/pdb2zz8/pdb
• Descriptor: LipL32 protein (2 entities in total)
• Functional Keywords: leptospira, outer-membrane protein, unknown function
• Biological source: Leptospira interrogans
• Total number of polymer chains: 2
• Total formula weight: 52960.12

Authors

Vivian, J.P.,Beddoe, T.,Rossjohn, J. (deposition date: 2009-02-06, release date: 2009-02-24, Last modification date: 2024-03-13)

Primary citation

Vivian, J.P.,Beddoe, T.,McAlister, A.D.,Wilce, M.C.,Zaker-Tabrizi, L.,Troy, S.,Byres, E.,Hoke, D.E.,Cullen, P.A.,Lo, M.,Murray, G.L.,Adler, B.,Rossjohn, J.
Crystal structure of LipL32, the most abundant surface protein of pathogenic Leptospira spp.
J.Mol.Biol., 387:1229-1238, 2009

PubMed Abstract: Spirochetes of the genus Leptospira cause leptospirosis in humans and animals worldwide. Proteins exposed on the bacterial cell surface are implicated in the pathogenesis of leptospirosis. However, the biological role of the majority of these proteins is unknown; this is principally due to the lack of genetic systems for investigating Leptospira and the absence of any structural information on leptospiral antigens. To address this, we have determined the 2.0-A-resolution structure of the lipoprotein LipL32, the most abundant outer-membrane and surface protein present exclusively in pathogenic Leptospira species. The extracellular domain of LipL32 revealed a compact, globular, "jelly-roll" fold from which projected an unusual extended beta-hairpin that served as a principal mediator of the observed crystallographic dimer. Two acid-rich patches were also identified as potential binding sites for positively charged ligands, such as laminin, to which LipL32 has a propensity to bind. Although LipL32 shared no significant sequence identity to any known protein, it possessed structural homology to the adhesins that bind components of the extracellular matrix, suggesting that LipL32 functions in an analogous manner. Moreover, the structure provides a framework for understanding the immunological role of this major surface lipoprotein.

PubMed: 19236879
DOI: 10.1016/j.jmb.2009.02.038

Experimental method

X-RAY DIFFRACTION (2.01 Å)