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Solution structure of the hypothetical protein Mth677 from Methanobacterium thermoautotrophicum : A novel α+β fold
Author(s) -
Blanco Francisco J.,
Yee Adelinda,
CamposOlivas Ramón,
Ortiz Ángel R.,
Devos Demian,
Valencia Alfonso,
Arrowsmith Cheryl H.,
Rico Manuel
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.04620504
Subject(s) - heteronuclear molecule , methanobacterium , escherichia coli , fold (higher order function) , protein structure , crystallography , computational biology , biology , structural genomics , chemistry , biochemistry , nuclear magnetic resonance spectroscopy , gene , stereochemistry , archaea , computer science , programming language
The structure of Mth677, a hypothetical protein from Methanobacterium thermoautotrophicum ( Mth ), has been determined by using heteronuclear nuclear magnetic resonance (NMR) methods on a double‐labeled 15 N‐ 13 C sample. Mth677 adopts a novel α+β fold, consisting of two α‐helices (one N terminal and one C terminal) packed on the same side of a central β‐hairpin. This structure is likely shared by its three orthologs, detected in three other Archaebacteria. There are no clear features in the sequences of these proteins or in the genome organization of Mth to make a reliable functional assignment to this protein. However, the structural similarity to Escherichia coli MinE, the protein which controls that division occurs at the midcell site, lends support to the proposal that Mth677 might be, in Mth , the counterpart of the topological specificity domain of MinE in E. coli .