2JFC

M144L mutant of Nitrite Reductase from Alcaligenes xylosoxidans in space group P212121

Summary for 2JFC

• Entry DOI: 10.2210/pdb2jfc/pdb
• Related: 1BQ5 1GS6 1GS7 1GS8 1HAU 1HAW 1NDT 1OE1 1OE2 1OE3 1WA0 1WA1 1WA2 1WAE 2BO0 2BP0 2BP8
• Descriptor: DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE, COPPER (II) ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, electron transfer. nitrite reductase, denitrification, complex formation, mutant, copper, metal-binding, alcaligenes xylosoxidans
• Biological source: ACHROMOBACTER XYLOSOXIDANS
• Total number of polymer chains: 6
• Total formula weight: 219450.52

Authors

Paraskevopoulos, K.,Hough, M.A.,Sawers, R.G.,Eady, R.R.,Hasnain, S.S. (deposition date: 2007-01-31, release date: 2007-05-29, Last modification date: 2023-12-13)

Primary citation

Paraskevopoulos, K.,Hough, M.A.,Sawers, R.G.,Eady, R.R.,Hasnain, S.S.
The Structure of the met144Leu Mutant of Copper Nitrite Reductase from Alcaligenes Xylosoxidans Provides the First Glimpse of a Protein-Protein Complex with Azurin II.
J.Biol.Inorg.Chem., 12:789-, 2007

PubMed Abstract: Cu-containing nitrite reductases (NiRs) perform the reduction of nitrite to NO via an ordered mechanism in which the delivery of a proton and an electron to the catalytic type 2 Cu site is highly orchestrated. Electron transfer from a redox partner protein, azurin or pseudoazurin, to the type 1 Cu site is assumed to occur through the formation of a protein-protein complex. We report here a new crystal form in space group P2(1)2(1)2(1) of the Met144Leu mutant of NiR from Alcaligenes xylosoxidans (AxNiR), revealing a head-to-head packing motif involving residues around the hydrophobic patch of domain 1. Superposition of the structure of azurin II with that of domain 1 of one of the Met144Leu molecules provides the first glimpse of an azurin II-NiR protein-protein complex. Mutations of two of the residues of AxNiR, Trp138His (Barrett et al. in Biochemistry 43:16311-16319, 2004) and Met87Leu, highlighted in the AxNiR-azurin complex, results in substantially decreased activity when azurin is used as the electron donor instead of methyl viologen, providing direct evidence for the importance of this region for complex formation.

PubMed: 17503096
DOI: 10.1007/S00775-007-0233-Y

Experimental method

X-RAY DIFFRACTION (2.4 Å)