3frl

The 2.25 A crystal structure of LipL32, the major surface antigen of Leptospira interrogans serovar Copenhageni

spinqualitylabelsall models 3frl, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3frl is a 2 chain structure with sequence from Leptospira interrogans serovar Copenhageni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: 211, CL, MSE, OXL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q72SM7_LEPIC Publication Abstract from PubMed Leptospirosis, a spirochaetal zoonotic disease caused by Leptospira, has been recognized as an important emerging infectious disease. LipL32 is the major exposed outer membrane protein found exclusively in pathogenic leptospires, where it accounts for up to 75% of the total outer membrane proteins. It is highly immunogenic, and recent studies have implicated LipL32 as an extracellular matrix binding protein, interacting with collagens, fibronectin, and laminin. In order to better understand the biological role and the structural requirements for the function of this important lipoprotein, we have determined the 2.25-A-resolution structure of recombinant LipL32 protein corresponding to residues 21-272 of the wild-type protein (LipL32(21-272)). The LipL32(21-272) monomer is made of a jelly-roll fold core from which several peripheral secondary structures protrude. LipL32(21-272) is structurally similar to several other jelly-roll proteins, some of which bind calcium ions and extracellular matrix proteins. Indeed, spectroscopic data (circular dichroism, intrinsic tryptophan fluorescence, and extrinsic 1-amino-2-naphthol-4-sulfonic acid fluorescence) confirmed the calcium-binding properties of LipL32(21-272). Ca(2+) binding resulted in a significant increase in the thermal stability of the protein, and binding was specific for Ca(2+) as no structural or stability perturbations were observed for Mg(2+), Zn(2+), or Cu(2+). Careful examination of the crystallographic structure suggests the locations of putative regions that could mediate Ca(2+) binding as well as binding to other interacting host proteins, such as collagens, fibronectin, and laminin. Structure and calcium-binding activity of LipL32, the major surface antigen of pathogenic Leptospira sp.,Hauk P, Guzzo CR, Roman Ramos H, Ho PL, Farah CS J Mol Biol. 2009 Jul 24;390(4):722-36. Epub 2009 May 25. PMID:19477185 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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