1hxv
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(New page: 200px<br /><applet load="1hxv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hxv" /> '''PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM T...)
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Revision as of 14:46, 20 November 2007
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PPIASE DOMAIN OF THE MYCOPLASMA GENITALIUM TRIGGER FACTOR
Overview
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.
About this Structure
1HXV is a Single protein structure of sequence from Mycoplasma genitalium. Full crystallographic information is available from OCA.
Reference
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., Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Ruterjans H, Griesinger C, Fiebig KM, J Mol Biol. 2002 May 10;318(4):1097-115. PMID:12054805
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