3PAY
Crystal structure of a putative adhesin (BACOVA_04077) from Bacteroides ovatus at 2.50 A resolution
Summary for 3PAY
| Entry DOI | 10.2210/pdb3pay/pdb |
| Descriptor | putative adhesin, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, cell adhesion |
| Biological source | Bacteroides ovatus |
| Total number of polymer chains | 4 |
| Total formula weight | 144655.56 |
| Authors | Joint Center for Structural Genomics (JCSG) (deposition date: 2010-10-19, release date: 2010-11-10, Last modification date: 2024-11-06) |
| Primary citation | Xu, Q.,Shoji, M.,Shibata, S.,Naito, M.,Sato, K.,Elsliger, M.A.,Grant, J.C.,Axelrod, H.L.,Chiu, H.J.,Farr, C.L.,Jaroszewski, L.,Knuth, M.W.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Curtis, M.A.,Nakayama, K.,Wilson, I.A. A Distinct Type of Pilus from the Human Microbiome. Cell, 165:690-703, 2016 Cited by PubMed Abstract: Pili are proteinaceous polymers of linked pilins that protrude from the cell surface of many bacteria and often mediate adherence and virulence. We investigated a set of 20 Bacteroidia pilins from the human microbiome whose structures and mechanism of assembly were unknown. Crystal structures and biochemical data revealed a diverse protein superfamily with a common Greek-key β sandwich fold with two transthyretin-like repeats that polymerize into a pilus through a strand-exchange mechanism. The assembly mechanism of the central, structural pilins involves proteinase-assisted removal of their N-terminal β strand, creating an extended hydrophobic groove that binds the C-terminal donor strands of the incoming pilin. Accessory pilins at the tip and base have unique structural features specific to their location, allowing initiation or termination of the assembly. The Bacteroidia pilus, therefore, has a biogenesis mechanism that is distinct from other known pili and likely represents a different type of bacterial pilus. PubMed: 27062925DOI: 10.1016/j.cell.2016.03.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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