3KLQ
Crystal Structure of the Minor Pilin FctB from Streptococcus pyogenes 90/306S
Summary for 3KLQ
| Entry DOI | 10.2210/pdb3klq/pdb |
| Descriptor | Putative pilus anchoring protein, GLYCEROL (3 entities in total) |
| Functional Keywords | cnab fold, inverse igg fold, polyproline-ii-like helix, cell adhesion |
| Biological source | Streptococcus pyogenes |
| Total number of polymer chains | 2 |
| Total formula weight | 31117.01 |
| Authors | Linke, C.,Young, P.G.,Bunker, R.D.,Caradoc-Davies, T.T.,Baker, E.N. (deposition date: 2009-11-08, release date: 2010-04-28, Last modification date: 2024-03-20) |
| Primary citation | Linke, C.,Young, P.G.,Kang, H.J.,Bunker, R.D.,Middleditch, M.J.,Caradoc-Davies, T.T.,Proft, T.,Baker, E.N. Crystal structure of the minor pilin FctB reveals determinants of Group A streptococcal pilus anchoring J.Biol.Chem., 285:20381-20389, 2010 Cited by PubMed Abstract: Cell surface pili are polymeric protein assemblies that enable bacteria to adhere to surfaces and to specific host tissues. The pili expressed by Gram-positive bacteria constitute a unique paradigm in which sortase-mediated covalent linkages join successive pilin subunits like beads on a string. These pili are formed from two or three distinct types of pilin subunit, typically encoded in small gene clusters, often with their cognate sortases. In Group A streptococci (GAS), a major pilin forms the polymeric backbone, whereas two minor pilins are located at the tip and the base. Here, we report the 1.9-A resolution crystal structure of the GAS basal pilin FctB, revealing an immunoglobulin (Ig)-like N-terminal domain with an extended proline-rich tail. Unexpected structural homology between the FctB Ig-like domain and the N-terminal domain of the GAS shaft pilin helps explain the use of the same sortase for polymerization of the shaft and its attachment to FctB. It also enabled the identification, from mass spectral data, of the lysine residue involved in the covalent linkage of FctB to the shaft. The proline-rich tail forms a polyproline-II helix that appears to be a common feature of the basal (cell wall-anchoring) pilins. Together, our results indicate distinct structural elements in the pilin proteins that play a role in selecting for the appropriate sortases and thereby help orchestrate the ordered assembly of the pilus. PubMed: 20427291DOI: 10.1074/jbc.M109.089680 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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