|
|
| (One intermediate revision by the same user not shown) |
| Line 1: |
Line 1: |
|
| |
|
| ==Cell surface anchoring domain== | | ==Cell surface anchoring domain== |
| <StructureSection load='5ix9' size='340' side='right'caption='[[5ix9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='5ix9' size='340' side='right'caption='[[5ix9]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5ix9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Jcm_11775 Jcm 11775]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IX9 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5ix9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinomonas_primoryensis Marinomonas primoryensis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IX9 FirstGlance]. <br> |
| </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=5ix9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ix9 OCA], [http://pdbe.org/5ix9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ix9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ix9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ix9 ProSAT]</span></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5ix9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ix9 OCA], [https://pdbe.org/5ix9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ix9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ix9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ix9 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/A1YIY2_9GAMM A1YIY2_9GAMM] |
| 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.
| |
| | |
| 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>
| |
| | |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 5ix9" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| *[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]] | | *[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Jcm 11775]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Guo, S]] | | [[Category: Marinomonas primoryensis]] |
| [[Category: Langelaan, D]] | | [[Category: Guo S]] |
| [[Category: Antifreeze protein]] | | [[Category: Langelaan D]] |
| [[Category: Biofilm-associated protein]]
| |
| [[Category: Cell adhesion]]
| |
| [[Category: Ice-binding protein]]
| |