5JUH
Crystal structure of C-terminal domain (RV) of MpAFP
Summary for 5JUH
| Entry DOI | 10.2210/pdb5juh/pdb |
| Descriptor | Antifreeze protein, CALCIUM ION (3 entities in total) |
| Functional Keywords | cell adhesion, rtx, antifreeze protein, type i secretion |
| Biological source | Marinomonas primoryensis |
| Total number of polymer chains | 1 |
| Total formula weight | 21511.41 |
| Authors | |
| Primary citation | Guo, S.,Stevens, C.A.,Vance, T.D.R.,Olijve, L.L.C.,Graham, L.A.,Campbell, R.L.,Yazdi, S.R.,Escobedo, C.,Bar-Dolev, M.,Yashunsky, V.,Braslavsky, I.,Langelaan, D.N.,Smith, S.P.,Allingham, J.S.,Voets, I.K.,Davies, P.L. Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice. Sci Adv, 3:e1701440-e1701440, 2017 Cited by PubMed Abstract: Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium 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-μm-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 β-sandwich domains that rigidify on binding Ca 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. PubMed: 28808685DOI: 10.1126/sciadv.1701440 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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