|Journal of Molecular Biology (2000) 302(1):189-203|
|Northeast Structural Genomics Consortium|
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The structure of MTH538, a previously uncharacterized hypothetical protein from Methanobacterium thermoautotrophicum, has been determined by NMR spectroscopy. ...
MTH538 is one of numerous structural genomics targets selected in a genome-wide survey of uncharacterized sequences from this organism. MTH538 is a so-called singleton, a sequence not closely related to any other (known) sequences. The structure of MTH538 closely resembles the known structures of receiver domains from two component response regulator systems, such as CheY, and is similar to the structures of flavodoxins and GTP-binding proteins. Tests on MTH538 for characteristic activities of CheY and flavodoxin were negative. MTH538 did not become phosphorylated in the presence of acetyl phosphate and Mg(2+), although it appeared to bind Mg(2+). MTH538 also did not bind flavin mononucleotide (FMN) or coenzyme F(420). Nevertheless, sequence and structure parallels between MTH538/CheY and two families of ATPase/phosphatase proteins suggest that MTH538 may have a role in a phosphorylation-independent two-component response regulator system.
|metabolism chemistry genetics analogs & derivatives classification |
|Protein Structure, Tertiary Amino Acid Sequence Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Secondary Computational Biology Sequence Alignment Bacterial Proteins Nuclear Magnetic Resonance, Biomolecular Phosphorylation Methanobacterium Structure-Activity Relationship Magnesium Membrane Proteins Adenosine Triphosphatases Flavin Mononucleotide Phosphoric Monoester Hydrolases Flavodoxin Riboflavin |
|18 (Last update: 11/17/2018 1:24:46pm)|
|J Mol Biol. 2000 Sep 8;302(1):189-203.|