1ZXJ

Crystal structure of the hypthetical Mycoplasma protein, MPN555

Summary for 1ZXJ

• Entry DOI: 10.2210/pdb1zxj/pdb
• Descriptor: Hypothetical protein MG377 homolog (2 entities in total)
• Functional Keywords: mostly alpha helical protein, tri-lobal structure, structural genomics, psi, protein structure initiative, berkeley structural genomics center, bsgc, unknown function
• Biological source: Mycoplasma pneumoniae
• Total number of polymer chains: 4
• Total formula weight: 101807.60

Authors

Schulze-Gahmen, U.,Aono, S.,Shengfeng, C.,Yokota, H.,Kim, R.,Kim, S.-H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2005-06-08, release date: 2005-07-26, Last modification date: 2024-02-14)

Primary citation

Schulze-Gahmen, U.,Aono, S.,Chen, S.,Yokota, H.,Kim, R.,Kim, S.H.
Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function.
Acta Crystallogr.,Sect.D, 61:1343-1347, 2005

PubMed Abstract: 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.

PubMed: 16204885
DOI: 10.1107/S090744490502264X

Experimental method

X-RAY DIFFRACTION (2.8 Å)