| Literature DB >> 12021439 |
Dinesh Christendat1, Vivian Saridakis, Youngchang Kim, Ponni A Kumar, Xiaohui Xu, Anthony Semesi, Andzrej Joachimiak, Cheryl H Arrowsmith, Aled M Edwards.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2002 PMID: 12021439 PMCID: PMC2373630 DOI: 10.1110/ps.4720102
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725