title: Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function.
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.
authors.affiliation: Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
authors.forename: Ursula
authors.initials: U
authors.lastname: Schulze-Gahmen
authors.forename: Shelly
authors.initials: S
authors.lastname: Aono
authors.forename: Shengfeng
authors.initials: S
authors.lastname: Chen
authors.forename: Hisao
authors.initials: H
authors.lastname: Yokota
authors.forename: Rosalind
authors.initials: R
authors.lastname: Kim
authors.forename: Sung Hou
authors.initials: SH
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D017931:DNA Primers / Q000737:chemistry; D004583:Electrons; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D009174:Mycoplasma / Q000378:metabolism*; D019696:Peptidylprolyl Isomerase / Q000737:chemistry* / Q000378:metabolism; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011549:Pseudomonas / Q000378:metabolism; D014509:Ureaplasma / Q000378:metabolism; D014734:Vibrio cholerae / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D002352:Carrier Proteins; D017931:DNA Primers; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C490900:SurA protein, E coli; D019696:Peptidylprolyl Isomerase