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NMR structure of hypothetical protein MG354 from Mycoplasma genitalium
Author(s) -
Pelton Jeffrey G.,
Shi Jianxia,
Yokota Hisao,
Kim Rosalind,
Wemmer David E.
Publication year - 2005
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20495
Subject(s) - mycoplasma genitalium , dihedral angle , protein structure , refseq , gene , structural genomics , crystallography , conformational isomerism , biology , computational biology , chemistry , genetics , hydrogen bond , genome , molecule , virology , biochemistry , chlamydia trachomatis , organic chemistry
Mycoplasma genitalium (Mg) and M. pneumoniae (Mp) are human pathogens with two of the smallest genomes sequenced to date ({approx} 480 and 680 genes, respectively). The Berkeley Structural Genomics Center is determining representative structures for gene products in these organisms, helping to understand the set of protein folds needed to sustain this minimal organism. The protein coded by gene MG354 (gi3844938) from M. genitalium has a relatively unique sequence, related only to MPN530 from M. pneumoniae (68% identity, coverage 99%) and MGA{_}0870 from the avian pathogen M. gallisepticum (23% identity, coverage 94%), has no homologue with a determined structure, and no functional annotations.