Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
References
- ↑ Schulze-Gahmen U, Aono S, Chen S, Yokota H, Kim R, Kim SH. Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function. Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1343-7. Epub 2005, Sep 28. PMID:16204885 doi:10.1107/S090744490502264X
