View source for 4u08


==Structure of Leptospira interrogans LRR protein LIC11098==
<StructureSection load='4u08' size='340' side='right'caption='[[4u08]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4u08]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptospira_interrogans_serovar_Copenhageni_str._Fiocruz_L1-130 Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U08 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4u08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u08 OCA], [https://pdbe.org/4u08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u08 RCSB], [https://www.ebi.ac.uk/pdbsum/4u08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u08 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q72TC3_LEPIC Q72TC3_LEPIC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogenic Leptospira spp. are the agents of leptospirosis, an emerging zoonotic disease. Analyses of Leptospira genomes have shown that the pathogenic leptospires (but not the saprophytes) possess a large number of genes encoding proteins containing leucine-rich repeat (LRR) domains. In other pathogenic bacteria, proteins with LRR domains have been shown to be involved in mediating host-cell attachment and invasion, but their functions remain unknown in Leptospira. To gain insight into the potential function of leptospiral LRR proteins, the crystal structures of four LRR proteins that represent a novel subfamily with consecutive stretches of a 23-amino-acid LRR repeat motif have been solved. The four proteins analyzed adopt the characteristic alpha/beta-solenoid horseshoe fold. The exposed residues of the inner concave surfaces of the solenoid, which constitute a putative functional binding site, are not conserved. The various leptospiral LRR proteins could therefore recognize distinct structural motifs of different host proteins and thus serve separate and complementary functions in the physiology of these bacteria.

Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans.,Miras I, Saul F, Nowakowski M, Weber P, Haouz A, Shepard W, Picardeau M Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1351-9. doi:, 10.1107/S139900471500704X. Epub 2015 May 23. PMID:26057675<ref>PMID:26057675</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4u08" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130]]
[[Category: Haouz A]]
[[Category: Picardeau M]]
[[Category: Saul FA]]
[[Category: Shepard W]]