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< | ==Crystal structure of functional region of UafA from Staphylococcus saprophyticus in P212121 form== | ||
<StructureSection load='3irz' size='340' side='right'caption='[[3irz]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3irz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_saprophyticus_subsp._saprophyticus_ATCC_15305_=_NCTC_7292 Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 = NCTC 7292]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IRZ 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]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3irz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3irz OCA], [https://pdbe.org/3irz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3irz RCSB], [https://www.ebi.ac.uk/pdbsum/3irz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3irz ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UAFA_STAS1 UAFA_STAS1] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ir/3irz_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/main_output.php?pdb_ID=3irz ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 3irz" style="background-color:#fffaf0;"></div> | |||
[[Category: Staphylococcus saprophyticus subsp. saprophyticus | == References == | ||
[[Category: Kuroda | <references/> | ||
[[Category: Matsuoka | __TOC__ | ||
[[Category: Shouji | </StructureSection> | ||
[[Category: Tanaka | [[Category: Large Structures]] | ||
[[Category: Tanaka | [[Category: Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 = NCTC 7292]] | ||
[[Category: Yao | [[Category: Kuroda M]] | ||
[[Category: Matsuoka E]] | |||
[[Category: Shouji Y]] | |||
[[Category: Tanaka I]] | |||
[[Category: Tanaka Y]] | |||
[[Category: Yao M]] | |||
Latest revision as of 19:02, 1 November 2023
Crystal structure of functional region of UafA from Staphylococcus saprophyticus in P212121 formCrystal structure of functional region of UafA from Staphylococcus saprophyticus in P212121 form
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStaphylococci 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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