1EO1

Solution structure of hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum

Summary for 1EO1

• Entry DOI: 10.2210/pdb1eo1/pdb
• Related: 1EIW
• Descriptor: HYPOTHETICAL PROTEIN MTH1175 (1 entity in total)
• Functional Keywords: mixed a/b protein, mixed beta sheet, strand order 321456, strands 2 and 6 antiparallel to rest., structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 1
• Total formula weight: 13175.89

Authors

Cort, J.R.,Arrowsmith, C.H.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2000-03-21, release date: 2000-12-20, Last modification date: 2024-05-22)

Primary citation

Cort, J.R.,Yee, A.,Edwards, A.M.,Arrowsmith, C.H.,Kennedy, M.A.
NMR Structure Determination and Structure-Based Functional Characterization of Conserved Hypothetical Protein MTH1175 from Methanobacterium Thermoautotrophicum
J.STRUCT.FUNCT.GENOM., 1:15-25, 2000

PubMed Abstract: The solution structure of MTH1175, a 124-residue protein from the archaeon Methanobacterium thermoautotrophicum has been determined by NMR spectroscopy. MTH1175 is part of a family of conserved hypothetical proteins (COG1433) with unknown functions which contains multiple paralogs from all complete archaeal genomes and the archaeal gene-rich bacterium Thermotoga maritima. Sequence similarity indicates this protein family may be related to the nitrogen fixation proteins NifB and NifX. MTH1175 adopts an alpha/beta topology with a single mixed beta-sheet, and contains two flexible loops and an unstructured C-terminal tail. The fold resembles that of Ribonuclease H and similar proteins, but differs from these in several respects, and is not likely to have a nuclease activity.

PubMed: 12836677
DOI: 10.1023/A:1011348803324

Experimental method

SOLUTION NMR