The crystal structure of hypothetical protein MTH1491 from Methanobacterium thermoautotrophicum

Protein Sci. 2002 Jun;11(6):1409-14. doi: 10.1110/ps.4720102.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / physiology
  • Binding Sites
  • Crystallography, X-Ray
  • Methanobacterium / chemistry*
  • Molecular Structure
  • Protein Conformation
  • Structure-Activity Relationship
  • Sulfates / chemistry
  • Sulfates / metabolism

Substances

  • Bacterial Proteins
  • Sulfates