3DA0
Crystal structure of a cleaved form of a chimeric receptor binding protein from Lactococcal phages subspecies TP901-1 and p2
Summary for 3DA0
| Entry DOI | 10.2210/pdb3da0/pdb |
| Related | 1zru 2bsd 2bse 2F0c |
| Descriptor | Cleaved chimeric receptor binding protein from bacteriophages TP901-1 and p2 (2 entities in total) |
| Functional Keywords | lactococcal phage p2, lactococcal phage tp901-1 receptor binding protein, viral protein |
| Biological source | Lactococcus phage TP901-1 More |
| Cellular location | Virion : Q71AW2 |
| Total number of polymer chains | 3 |
| Total formula weight | 44530.94 |
| Authors | Siponen, M.I.,Blangy, S.,Spinelli, S.,Vera, L.,Cambillau, C.,Campanacci, V. (deposition date: 2008-05-28, release date: 2009-06-09, Last modification date: 2023-08-30) |
| Primary citation | Siponen, M.,Spinelli, S.,Blangy, S.,Moineau, S.,Cambillau, C.,Campanacci, V. Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages. J.Bacteriol., 191:3220-3225, 2009 Cited by PubMed Abstract: Lactococcus lactis, a gram-positive bacterium widely used by the dairy industry to manufacture cheeses, is subject to infection by a diverse population of virulent phages. We have previously determined the structures of three receptor binding proteins (RBPs) from lactococcal phages TP901-1, p2, and bIL170, each of them having a distinct host range. Virulent phages p2 and bIL170 are classified within the 936 group, while the temperate phage TP901-1 is a member of the genetically distinct P335 polythetic group. These RBPs comprise three domains: the N-terminal domain, binding to the virion particle; a beta-helical linker domain; and the C-terminal domain, bearing the receptor binding site used for host recognition. Here, we have designed, expressed, and determined the structure of an RBP chimera in which the N-terminal and linker RBP domains of phage TP901-1 (P335) are fused to the C-terminal RBP domain of phage p2 (936). This chimera exhibits a stable structure that closely resembles the parental structures, while a slight displacement of the linker made RBP domain adaptation efficient. The receptor binding site is structurally indistinguishable from that of native p2 RBP and binds glycerol with excellent affinity. PubMed: 19286807DOI: 10.1128/JB.01637-08 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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