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3WIA

Crystal structure of the N-terminal 1-37 residues deleted mutant of Geobacillus copper nitrite reductase

Summary for 3WIA
Entry DOI10.2210/pdb3wia/pdb
Related3WI9
DescriptorNitrite reductase, COPPER (II) ION, FORMIC ACID, ... (4 entities in total)
Functional Keywordscupredoxin-fold, trimer, nitrite reduction, oxidoreductase
Biological sourceGeobacillus kaustophilus
Total number of polymer chains9
Total formula weight287197.92
Authors
Fukuda, Y.,Nojiri, M. (deposition date: 2013-09-09, release date: 2014-07-23, Last modification date: 2023-11-08)
Primary citationFukuda, Y.,Koteishi, H.,Yoneda, R.,Tamada, T.,Takami, H.,Inoue, T.,Nojiri, M.
Structural and functional characterization of the Geobacillus copper nitrite reductase: involvement of the unique N-terminal region in the interprotein electron transfer with its redox partner
Biochim.Biophys.Acta, 1837:396-405, 2014
Cited by
PubMed Abstract: The crystal structures of copper-containing nitrite reductase (CuNiR) from the thermophilic Gram-positive bacterium Geobacillus kaustophilus HTA426 and the amino (N)-terminal 68 residue-deleted mutant were determined at resolutions of 1.3Å and 1.8Å, respectively. Both structures show a striking resemblance with the overall structure of the well-known CuNiRs composed of two Greek key β-barrel domains; however, a remarkable structural difference was found in the N-terminal region. The unique region has one β-strand and one α-helix extended to the northern surface of the type-1 copper site. The superposition of the Geobacillus CuNiR model on the electron-transfer complex structure of CuNiR with the redox partner cytochrome c551 in other denitrifier system led us to infer that this region contributes to the transient binding with the partner protein during the interprotein electron transfer reaction in the Geobacillus system. Furthermore, electron-transfer kinetics experiments using N-terminal residue-deleted mutant and the redox partner, Geobacillus cytochrome c551, were carried out. These structural and kinetics studies demonstrate that the region is directly involved in the specific partner recognition.
PubMed: 24440558
DOI: 10.1016/j.bbabio.2014.01.004
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.77 Å)
Structure validation

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数据于2024-11-06公开中

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