Crystal Structure of LipL32, the Most Abundant Surface Protein of Pathogenic Leptospira spp

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...

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Veröffentlicht in:	Journal of molecular biology 2009-04, Vol.387 (5), p.1229-1238
Hauptverfasser:	Vivian, Julian P., Beddoe, Travis, McAlister, Adrian D., Wilce, Matthew C.J., Zaker-Tabrizi, Leyla, Troy, Sally, Byres, Emma, Hoke, David E., Cullen, Paul A., Lo, Miranda, Murray, Gerald L., Adler, Ben, Rossjohn, Jamie
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antigens, Bacterial - chemistry Antigens, Bacterial - genetics Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - immunology Base Sequence Binding Sites Crystallography, X-Ray Dimerization DNA Primers - genetics DNA, Bacterial - genetics Humans jelly-roll fold Leptospira Leptospira - chemistry Leptospira - genetics Leptospira - immunology Leptospira - pathogenicity LipL32 Lipoproteins - chemistry Lipoproteins - genetics Lipoproteins - immunology Models, Molecular outer-membrane protein Protein Conformation Protein Structure, Quaternary Protein Structure, Tertiary Recombinant Proteins - chemistry Recombinant Proteins - genetics Static Electricity
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