1QLM

The crystal structure of methenyltetrahydromethanopterin cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri

Summary for 1QLM

Entry DOI	10.2210/pdb1qlm/pdb
Descriptor	METHENYLTETRAHYDROMETHANOPTERIN CYCLOHYDROLASE, PHOSPHATE ION (3 entities in total)
Functional Keywords	methanogenesis, biological methanogenesis, hydrolase, tetrahydromethanopterin
Biological source	METHANOPYRUS KANDLERI
Cellular location	Cytoplasm: P94954
Total number of polymer chains	1
Total formula weight	34378.79
Authors	Grabarse, W. (deposition date: 1999-09-01, release date: 1999-09-20, Last modification date: 2024-05-08)
Primary citation	Grabarse, W.,Vaupel, M.,Vorholt, J.A.,Shima, S.,Thauer, R.K.,Wittershagen, A.,Bourenkov, G.,Bartunik, H.D.,Ermler, U. The Crystal Structure of Methenyltetrahydromethano- Pterin Cyclohydrolase from the Hyperthermophilic Archaeon Methanopyrus Kandleri Structure, 7:1257-, 1999 Cited by PubMed Abstract: The reduction of carbon dioxide to methane in methanogenic archaea involves the tetrahydrofolate analogue tetrahydromethanopterin (H(4)MPT) as a C(1) unit carrier. In the third step of this reaction sequence, N(5)-formyl-H(4)MPT is converted to methenyl-H(4)MPT(+) by the enzyme methenyltetrahydromethanopterin cyclohydrolase. The cyclohydrolase from the hyperthermophilic archaeon Methanopyrus kandleri (Mch) is extremely thermostable and adapted to a high intracellular concentration of lyotropic salts. PubMed: 10545331 DOI: 10.1016/S0969-2126(00)80059-3 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation