3AYG

Crystal structure of nitric oxide reductase complex with HQNO

Summary for 3AYG

• Entry DOI: 10.2210/pdb3ayg/pdb
• Related: 3AYF
• Descriptor: Nitric oxide reductase, PROTOPORPHYRIN IX CONTAINING FE, ZINC ION, ... (8 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 95171.93

Authors

Matsumoto, Y.,Tosha, T.,Pisliakov, A.V.,Hino, T.,Sugimoti, H.,Nagano, S.,Sugita, Y.,Shiro, Y. (deposition date: 2011-05-06, release date: 2012-01-25, Last modification date: 2024-03-13)

Primary citation

Matsumoto, Y.,Tosha, T.,Pisliakov, A.V.,Hino, T.,Sugimoto, H.,Nagano, S.,Sugita, Y.,Shiro, Y.
Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus.
Nat.Struct.Mol.Biol., 19:238-245, 2012

PubMed Abstract: The structure of quinol-dependent nitric oxide reductase (qNOR) from G. stearothermophilus, which catalyzes the reduction of NO to produce the major ozone-depleting gas N(2)O, has been characterized at 2.5 Å resolution. The overall fold of qNOR is similar to that of cytochrome c-dependent NOR (cNOR), and some structural features that are characteristic of cNOR, such as the calcium binding site and hydrophilic cytochrome c domain, are observed in qNOR, even though it harbors no heme c. In contrast to cNOR, structure-based mutagenesis and molecular dynamics simulation studies of qNOR suggest that a water channel from the cytoplasm can serve as a proton transfer pathway for the catalytic reaction. Further structural comparison of qNOR with cNOR and aerobic and microaerobic respiratory oxidases elucidates their evolutionary relationship and possible functional conversions.

PubMed: 22266822
DOI: 10.1038/nsmb.2213

Experimental method

X-RAY DIFFRACTION (2.7 Å)