1zxj

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.