1FTR

FORMYLMETHANOFURAN:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE FROM METHANOPYRUS KANDLERI

Summary for 1FTR

• Entry DOI: 10.2210/pdb1ftr/pdb
• Descriptor: FORMYLMETHANOFURAN\:TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE (2 entities in total)
• Functional Keywords: formyltransferase, methanogenesis, archae, acyltransferase, hyperthermophilic, halophilic
• Biological source: Methanopyrus kandleri
• Total number of polymer chains: 4
• Total formula weight: 126745.80

Authors

Ermler, U.,Merckel, M.C.,Thauer, R.K.,Shima, S. (deposition date: 1997-09-21, release date: 1998-10-14, Last modification date: 2024-02-07)

Primary citation

Ermler, U.,Merckel, M.,Thauer, R.,Shima, S.
Formylmethanofuran: tetrahydromethanopterin formyltransferase from Methanopyrus kandleri - new insights into salt-dependence and thermostability.
Structure, 5:635-646, 1997

PubMed Abstract: Formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from the methanogenic Archaeon Methanopyrus kandleri (optimum growth temperature 98 degrees C) is a hyperthermophilic enzyme that is absolutely dependent on the presence of lyotropic salts for activity and thermostability. The enzyme is involved in the pathway of carbon dioxide reduction to methane and catalyzes the transfer of formyl from formylmethanofuran to tetrahydromethanopterin.

PubMed: 9195883
DOI: 10.1016/S0969-2126(97)00219-0

Experimental method

X-RAY DIFFRACTION (1.7 Å)