Christendat Dinesh, Saridakis Vivian, Kim Youngchang, Kumar Ponni A, Xu Xiaohui, Semesi Anthony, Joachimiak Andzrej, Arrowsmith Cheryl H, Edwards Aled M
Clinical Genomics Center, University Health Network, Toronto, Ontario, M5G 1L7, Canada.
Protein Sci. 2002 Jun;11(6):1409-14. doi: 10.1110/ps.4720102.
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.
作为我们结构蛋白质组学计划的一部分，我们已经确定了MTH1491的晶体结构，它是来自嗜热自养甲烷杆菌的一种先前未被表征的假定蛋白。MTH1491是在全基因组范围内对未表征蛋白进行调查时选择的众多结构基因组学目标之一。它属于一类生物学功能未知的蛋白质家族。MTH1491的晶体结构是该蛋白质家族的首个结构，由一个总体上具有51234链序的五链平行β折叠以及侧翼螺旋组成。从晶体接触和凝胶过滤研究来看，该分子的寡聚形式是三聚体。分析表明，MTH1491的结构与脱氢酶、酰胺水解酶和氧化还原酶的结构相似。通过序列和结构分析相结合的方法，我们表明MTH1491不属于蛋白质的脱氢酶或酰胺水解酶超家族。
