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Publication Abstract from PubMed
As part of our structural proteomics initiative, we have determined the crystal structure of MTH1491, a previously uncharacterized hypothetical protein from Methanobacterium thermoautotrophicum. MTH1491 is one of numerous structural genomics targets selected in a genome-wide survey of uncharacterized proteins. It belongs to a family of proteins whose biological function is not known. The crystal structure of MTH1491, the first structure for this family of proteins, consists of an overall five-stranded parallel beta-sheet with strand order 51234 and flanking helices. The oligomeric form of this molecule is a trimer as seen from both crystal contacts and gel filtration studies. Analysis revealed that the structure of MTH1491 is similar to that of dehydrogenases, amidohydrolases, and oxidoreductases. Using a combination of sequence and structural analyses, we showed that MTH1491 does not belong to either the dehydrogenase or the amidohydrolase superfamilies of proteins.
The crystal structure of hypothetical protein MTH1491 from Methanobacterium thermoautotrophicum.,Christendat D, Saridakis V, Kim Y, Kumar PA, Xu X, Semesi A, Joachimiak A, Arrowsmith CH, Edwards AM Protein Sci. 2002 Jun;11(6):1409-14. PMID:12021439[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Christendat D, Saridakis V, Kim Y, Kumar PA, Xu X, Semesi A, Joachimiak A, Arrowsmith CH, Edwards AM. The crystal structure of hypothetical protein MTH1491 from Methanobacterium thermoautotrophicum. Protein Sci. 2002 Jun;11(6):1409-14. PMID:12021439
