1HXV

PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM TRIGGER FACTOR

Summary for 1HXV

• Entry DOI: 10.2210/pdb1hxv/pdb
• Descriptor: TRIGGER FACTOR (1 entity in total)
• Functional Keywords: fkbp fold, ppiase, chaperone
• Biological source: Mycoplasma genitalium
• Total number of polymer chains: 1
• Total formula weight: 12456.36

Authors

Vogtherr, M.,Parac, T.N.,Maurer, M.,Pahl, A.,Fiebig, K. (deposition date: 2001-01-17, release date: 2002-05-29, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR