1zxj

From Proteopedia

Revision as of 05:36, 21 November 2007

Crystal structure of the hypthetical Mycoplasma protein, MPN555

Overview

The crystal structure of the hypothetical protein MPN555 from Mycoplasma, pneumoniae (gi|1673958) has been determined to a resolution of 2.8, Angstrom using anomalous diffraction data at the Se-peak wavelength., Structure determination revealed a mostly alpha-helical protein with a, three-lobed shape. The three lobes or fingers delineate a central binding, groove and additional grooves between lobes 1 and 3 and between lobes 2, and 3. For one of the molecules in the asymmetric unit, the central, binding pocket was filled with a peptide from the uncleaved N-terminal, affinity tag. The MPN555 structure has structural homology to two, bacterial chaperone proteins: SurA and trigger factor from Escherichia, coli. The structural data and the homology to other chaperone proteins, suggests an involvement in protein folding as a molecular chaperone for, MPN555.

About this Structure

1ZXJ is a Single protein structure of sequence from Mycoplasma pneumoniae. Full crystallographic information is available from OCA.

Reference

Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function., Schulze-Gahmen U, Aono S, Chen S, Yokota H, Kim R, Kim SH, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1343-7. Epub 2005, Sep 28. PMID:16204885

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