Ontology highlight
ABSTRACT:
SUBMITTER: Aufhammer SW
PROVIDER: S-EPMC2253363 | biostudies-literature | 2005 Jul
REPOSITORIES: biostudies-literature
Aufhammer Stephan W SW Warkentin Eberhard E Ermler Ulrich U Hagemeier Christoph H CH Thauer Rudolf K RK Shima Seigo S
Protein science : a publication of the Protein Society 20050603 7
Methylenetetratetrahydromethanopterin reductase (Mer) is involved in CO(2) reduction to methane in methanogenic archaea and catalyses the reversible reduction of methylenetetrahydromethanopterin (methylene-H(4)MPT) to methyl-H(4)MPT with coenzyme F(420)H(2), which is a reduced 5'-deazaflavin. Mer was recently established as a TIM barrel structure containing a nonprolyl cis-peptide bond but the binding site of the substrates remained elusive. We report here on the crystal structure of Mer in comp ...[more]