The crystal structure of hypothetical protein MTH1491 from Methanobacterium thermoautotrophicum |
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Authors: | Christendat Dinesh Saridakis Vivian Kim Youngchang Kumar Ponni A Xu Xiaohui Semesi Anthony Joachimiak Andzrej Arrowsmith Cheryl H Edwards Aled M |
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Institution: | Clinical Genomics Center, University Health Network, Toronto, Ontario, M5G 1L7, Canada. dinesh@uhnres.utoronto.ca |
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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. |
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Keywords: | Hypothetical protein structural proteomics X-ray crystallography structural biology |
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