1HXV

PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM TRIGGER FACTOR

1HXV の概要

• エントリーDOI: 10.2210/pdb1hxv/pdb
• 分子名称: TRIGGER FACTOR (1 entity in total)
• 機能のキーワード: fkbp fold, ppiase, chaperone
• 由来する生物種: Mycoplasma genitalium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12456.36

構造登録者

Vogtherr, M.,Parac, T.N.,Maurer, M.,Pahl, A.,Fiebig, K. (登録日: 2001-01-17, 公開日: 2002-05-29, 最終更新日: 2024-05-22)

主引用文献

Vogtherr, M.,Jacobs, D.M.,Parac, T.N.,Maurer, M.,Pahl, A.,Saxena, K.,Ruterjans, H.,Griesinger, C.,Fiebig, K.M.
NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.
J.Mol.Biol., 318:1097-1115, 2002

PubMed Abstract: We have solved the solution structure of the peptidyl-prolyl cis-trans isomerase (PPIase) domain of the trigger factor from Mycoplasma genitalium by homo- and heteronuclear NMR spectroscopy. Our results lead to a well-defined structure with a backbone rmsd of 0.23 A. As predicted, the PPIase domain of the trigger factor adopts the FK506 binding protein (FKBP) fold. Furthermore, our NMR relaxation data indicate that the dynamic behavior of the trigger factor PPIase domain and of FKBP are similar. Structural variations when compared to FKBP exist in the flap region and within the bulges of strand 5 of the beta sheet. Although the active-site crevice is similar to that of FKBP, subtle steric variations in this region can explain why FK506 does not bind to the trigger factor. Sequence variability (27% identity) between trigger factor and FKBP results in significant differences in surface charge distribution and the absence of the first strand of the central beta sheet. Our data indicate, however, that this strand may be partially structured as "nascent" beta strand. This makes the trigger factor PPIase domain the most minimal representative of the FKBP like protein family of PPIases.

PubMed: 12054805
DOI: 10.1016/S0022-2836(02)00112-2

実験手法

SOLUTION NMR