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5irb

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<StructureSection load='5irb' size='340' side='right'caption='[[5irb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5irb' size='340' side='right'caption='[[5irb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5irb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Jcm_11775 Jcm 11775]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IRB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5irb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinomonas_primoryensis Marinomonas primoryensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IRB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<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=5irb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5irb OCA], [http://pdbe.org/5irb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5irb RCSB], [http://www.ebi.ac.uk/pdbsum/5irb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5irb ProSAT]</span></td></tr>
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<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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5irb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5irb OCA], [https://pdbe.org/5irb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5irb RCSB], [https://www.ebi.ac.uk/pdbsum/5irb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5irb ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A1YIY2_9GAMM A1YIY2_9GAMM]
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Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and nutrients. We have reconstructed this 0.6-mum-long adhesin using a "dissect and build" structural biology approach and have established complementary roles for its five distinct regions. Domains in region I (RI) tether the adhesin to the type I secretion machinery in the periplasm of the bacterium and pass it through the outer membrane. RII comprises ~120 identical immunoglobulin-like beta-sandwich domains that rigidify on binding Ca2+ to project the adhesion regions RIII and RIV into the medium. RIII contains ligand-binding domains that join diatoms and bacteria together in a mixed-species community on the underside of sea ice where incident light is maximal. RIV is the ice-binding domain, and the terminal RV domain contains several "repeats-in-toxin" motifs and a noncleavable signal sequence that target proteins for export via the type I secretion system. Similar structural architecture is present in the adhesins of many pathogenic bacteria and provides a guide to finding and blocking binding domains to weaken infectivity.
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Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice.,Guo S, Stevens CA, Vance TDR, Olijve LLC, Graham LA, Campbell RL, Yazdi SR, Escobedo C, Bar-Dolev M, Yashunsky V, Braslavsky I, Langelaan DN, Smith SP, Allingham JS, Voets IK, Davies PL Sci Adv. 2017 Aug 9;3(8):e1701440. doi: 10.1126/sciadv.1701440. eCollection 2017 , Aug. PMID:28808685<ref>PMID:28808685</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5irb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Jcm 11775]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Campbell, R]]
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[[Category: Marinomonas primoryensis]]
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[[Category: Davies, P]]
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[[Category: Campbell R]]
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[[Category: Guo, S]]
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[[Category: Davies P]]
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[[Category: Phippen, S]]
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[[Category: Guo S]]
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[[Category: Biofilm-associated protein]]
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[[Category: Phippen S]]
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[[Category: Cell adhesion]]
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[[Category: Ice-binding protein]]
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[[Category: Rtx-adhesin]]
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Current revision

Structural insight into host cell surface retention of a 1.5-MDa bacterial ice-binding adhesin

PDB ID 5irb

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