1O75

Tp47, the 47-Kilodalton Lipoprotein of Treponema pallidum

1O75 の概要

• エントリーDOI: 10.2210/pdb1o75/pdb
• 分子名称: 47 KDA MEMBRANE ANTIGEN, 2,3-di-O-sulfo-alpha-D-glucopyranose-(1-6)-2,3-di-O-sulfo-alpha-D-glucopyranose, XENON, ... (4 entities in total)
• 機能のキーワード: lipoproteinullntigen, penicillin-binding protein, integral membrane lipoprotein, immunogen, four-domain protein, antigen, lipoprotein
• 由来する生物種: TREPONEMA PALLIDUM
• 細胞内の位置: Cell inner membrane ; Lipid-anchor : P29723
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92648.15

構造登録者

Deka, R.K.,Machius, M.,Norgard, M.V.,Tomchick, D.R. (登録日: 2002-10-23, 公開日: 2002-11-01, 最終更新日: 2024-05-08)

主引用文献

Deka, R.K.,Machius, M.,Norgard, M.V.,Tomchick, D.R.
Crystal structure of the 47-kDa lipoprotein of Treponema pallidum reveals a novel penicillin-binding protein.
J. Biol. Chem., 277:41857-41864, 2002

PubMed Abstract: Syphilis is a complex sexually transmitted disease caused by the spirochetal bacterium Treponema pallidum. T. pallidum has remained exquisitely sensitive to penicillin, but the mode of action and lethal targets for beta-lactams are still unknown. We previously identified the T. pallidum 47-kDa lipoprotein (Tp47) as a penicillin-binding protein (PBP). Tp47 contains three hypothetical consensus motifs (SVTK, TEN, and KTG) that typically form the active center of other PBPs. Yet, in this study, mutations of key amino acids within these motifs failed to abolish the penicillin binding activity of Tp47. The crystal structure of Tp47 at a resolution of 1.95 A revealed a fold different from any other known PBP; Tp47 is predominantly beta-sheet, in contrast to the alpha/beta-fold common to other PBPs. It comprises four distinct domains: two complex beta-sheet-containing N-terminal domains and two C-terminal domains that adopt immunoglobulin-like folds. The three hypothetical PBP signature motifs do not come together to form a typical PBP active site. Furthermore, Tp47 is unusual in that it displays beta-lactamase activity (k(cat) for penicillin = 271 +/- 6 s(-1)), a feature that hindered attempts to identify the active site in Tp47 by co-crystallization and mass spectrometric techniques. Taken together, Tp47 does not fit the classical structural and mechanistic paradigms for PBPs, and thus Tp47 appears to represent a new class of PBP.

PubMed: 12196546
DOI: 10.1074/jbc.M207402200

実験手法

X-RAY DIFFRACTION (1.95 Å)