The crystal structure of hypothetical protein MTH1491 from Methanobacterium thermoautotrophicum.
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.
Christendat
Dinesh
D
Clinical Genomics Center, University Health Network, Toronto, Ontario, M5G 1L7, Canada. dinesh@uhnres.utoronto.ca
Saridakis
Vivian
V
Kim
Youngchang
Y
Kumar
Ponni A
PA
Xu
Xiaohui
X
Semesi
Anthony
A
Joachimiak
Andzrej
A
Arrowsmith
Cheryl H
CH
Edwards
Aled M
AM
D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology; D001665:Binding Sites; D018360:Crystallography, X-Ray; D017014:Methanobacterium / Q000737:chemistry*; D015394:Molecular Structure; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013431:Sulfates / Q000737:chemistry / Q000378:metabolism
D001426:Bacterial Proteins; D013431:Sulfates