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==Crystal structure of functional region of UafA from Staphylococcus saprophyticus at 1.50 angstrom resolution==
==Crystal structure of functional region of UafA from Staphylococcus saprophyticus at 1.50 angstrom resolution==
<StructureSection load='3irp' size='340' side='right' caption='[[3irp]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='3irp' size='340' side='right' caption='[[3irp]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3irp]] 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=3IRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IRP FirstGlance]. <br>
<table><tr><td colspan='2'>[[3irp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Stas1 Stas1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IRP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IRP 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>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3irz|3irz]], [[3is0|3is0]], [[3is1|3is1]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3irz|3irz]], [[3is0|3is0]], [[3is1|3is1]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uafA, SSP0135 ([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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uafA, SSP0135 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=342451 STAS1])</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=3irp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3irp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3irp RCSB], [http://www.ebi.ac.uk/pdbsum/3irp PDBsum]</span></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=3irp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3irp OCA], [http://pdbe.org/3irp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3irp RCSB], [http://www.ebi.ac.uk/pdbsum/3irp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3irp ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3irp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3irp" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Staphylococcus saprophyticus subsp. saprophyticus atcc 15305]]
[[Category: Stas1]]
[[Category: Kuroda, M]]
[[Category: Kuroda, M]]
[[Category: Matsuoka, E]]
[[Category: Matsuoka, E]]

Revision as of 00:08, 6 August 2016

Crystal structure of functional region of UafA from Staphylococcus saprophyticus at 1.50 angstrom resolutionCrystal structure of functional region of UafA from Staphylococcus saprophyticus at 1.50 angstrom resolution

Structural highlights

3irp is a 1 chain structure with sequence from Stas1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:uafA, SSP0135 (STAS1)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

3irp, resolution 1.50Å

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