3is1

<StructureSection load='3is1' size='340' side='right' caption='[[3is1]], [[Resolution|resolution]] 2.45&Aring;' scene=''>

<table><tr><td colspan='2'>[[3is1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_saprophyticus_subsp._saprophyticus_atcc_15305 Staphylococcus saprophyticus subsp. saprophyticus atcc 15305]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IS1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IS1 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3irp|3irp]], [[3irz|3irz]], [[3is0|3is0]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSP0135, uafA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=342451 Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3is1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3is1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3is1 RCSB], [http://www.ebi.ac.uk/pdbsum/3is1 PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/is/3is1_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

Staphylococci use cell wall-anchored proteins as adhesins to attach to host tissues. Staphylococcus saprophyticus, a uropathogenic species, has a unique cell wall-anchored protein, uro-adherence factor A (UafA), which shows erythrocyte binding activity. To investigate the mechanism of adhesion by UafA, we determined the crystal structure of the functional region of UafA at 1.5 A resolution. The structure was composed of three domains, designated as the N2, N3, and B domains, arranged in a triangular relative configuration. Hemagglutination inhibition assay with domain-truncated mutants indicated that both N and B domains were necessary for erythrocyte binding. Based on these results, a novel manner of ligand binding in which the B domain acts as a functional domain was proposed as the adhesion mechanism of S. saprophyticus.

Crystal structure of the functional region of Uro-adherence factor A from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding.,Matsuoka E, Tanaka Y, Kuroda M, Shouji Y, Ohta T, Tanaka I, Yao M Protein Sci. 2011 Feb;20(2):406-16. doi: 10.1002/pro.573. PMID:21280131<ref>PMID:21280131</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Staphylococcus saprophyticus subsp. saprophyticus atcc 15305]]

[[Category: Kuroda, M]]

[[Category: Matsuoka, E]]

[[Category: Shouji, Y]]

[[Category: Tanaka, I]]

[[Category: Tanaka, Y]]

[[Category: Yao, M]]

[[Category: Virulence]]