5ix9: Difference between revisions
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==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]], [[NMR_Ensembles_of_Models | 20 NMR models]]' 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 [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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5ix9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5ix9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Jcm 11775]] | [[Category: Jcm 11775]] | ||
[[Category: Large Structures]] | |||
[[Category: Guo, S]] | [[Category: Guo, S]] | ||
[[Category: Langelaan, D]] | [[Category: Langelaan, D]] | ||
Revision as of 11:05, 8 January 2020
Cell surface anchoring domainCell surface anchoring domain
Structural highlights
Publication Abstract from PubMedBacterial 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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