3EJC

Full length Receptor Binding Protein from Lactococcal phage TP901-1

3EJC の概要

• エントリーDOI: 10.2210/pdb3ejc/pdb
• 関連するPDBエントリー: 2f0c 3d8m 3da0
• 分子名称: Baseplate protein (BPP) (2 entities in total)
• 機能のキーワード: lactococcus lactis, siphoviridae, receptor binding protein, phage tp901-1, p335 species, viral protein, sugar binding protein
• 由来する生物種: Lactococcus phage TP901-1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17994.12

構造登録者

Spinelli, S.,Lichiere, J.,Blangy, S.,Sciara, G.,Cambillau, C.,Campanacci, V. (登録日: 2008-09-18, 公開日: 2009-10-06, 最終更新日: 2023-08-30)

主引用文献

Bebeacua, C.,Bron, P.,Lai, L.,Vegge, C.S.,Brondsted, L.,Spinelli, S.,Campanacci, V.,Veesler, D.,van Heel, M.,Cambillau, C.
Structure and molecular assignment of lactococcal phage TP901-1 baseplate.
J.Biol.Chem., 285:39079-39086, 2010

PubMed Abstract: P335 lactococcal phages infect the gram(+) bacterium Lactococcus lactis using a large multiprotein complex located at the distal part of the tail and termed baseplate (BP). The BP harbors the receptor-binding proteins (RBPs), which allow the specific recognition of saccharidic receptors localized on the host cell surface. We report here the electron microscopic structure of the phage TP901-1 wild-type BP as well as those of two mutants bppL (-) and bppU(-), lacking BppL (the RBPs) or both peripheral BP components (BppL and BppU), respectively. We also achieved an electron microscopic reconstruction of a partial BP complex, formed by BppU and BppL. This complex exhibits a tripod shape and is composed of nine BppLs and three BppUs. These structures, combined with light-scattering measurements, led us to propose that the TP901-1 BP harbors six tripods at its periphery, located around the central tube formed by ORF46 (Dit) hexamers, at its proximal end, and a ORF47 (Tal) trimer at its distal extremity. A total of 54 BppLs (18 RBPs) are thus available to mediate host anchoring with a large apparent avidity. TP901-1 BP exhibits an infection-ready conformation and differs strikingly from the lactococcal phage p2 BP, bearing only 6 RBPs, and which needs a conformational change to reach its activated state. The comparison of several Siphoviridae structures uncovers a close organization of their central BP core whereas striking differences occur at the periphery, leading to diverse mechanisms of host recognition.

PubMed: 20937834
DOI: 10.1074/jbc.M110.175646

実験手法

X-RAY DIFFRACTION (1.85 Å)