1KQF

FORMATE DEHYDROGENASE N FROM E. COLI

Summary for 1KQF

• Entry DOI: 10.2210/pdb1kqf/pdb
• Related: 1KQG
• Descriptor: FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT, FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, IRON-SULFUR SUBUNIT, FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, CYTOCHROME B556(FDN) SUBUNIT, ... (9 entities in total)
• Functional Keywords: oxidoreductase, selenium, selenocysteine, secys, molybdenum, molybdopterin, mpt, molybdopterin guanine dinucleotide, mgd, iron sulfur cluster, fe4s4, formate, dehydrogenase, anaerobic, integral membrane protein
• Biological source: Escherichia coli; More
• Cellular location: Periplasm: P24183; Cell inner membrane; Single-pass membrane protein: P0AAJ3
• Total number of polymer chains: 3
• Total formula weight: 176805.74

Authors

Jormakka, M.,Tornroth, S.,Byrne, B.,Iwata, S. (deposition date: 2002-01-05, release date: 2002-03-15, Last modification date: 2024-02-14)

Primary citation

Jormakka, M.,Tornroth, S.,Byrne, B.,Iwata, S.
Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.
Science, 295:1863-1868, 2002

PubMed Abstract: The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.

PubMed: 11884747
DOI: 10.1126/science.1068186

Experimental method

X-RAY DIFFRACTION (1.6 Å)