1OE1

Atomic Resolution Structure of the Wildtype Native Nitrite Reductase from Alcaligenes xylosoxidans

Summary for 1OE1

• Entry DOI: 10.2210/pdb1oe1/pdb
• Related: 1BQ5 1GS6 1GS7 1GS8 1HAU 1HAW 1NDT 1OE2
• Descriptor: DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE, COPPER (II) ION, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: reductase, denitrification, nitrite reductase
• Biological source: ALCALIGENES XYLOSOXIDANS
• Total number of polymer chains: 1
• Total formula weight: 36874.81

Authors

Ellis, M.J.,Dodd, F.E.,Hasnain, S.S. (deposition date: 2003-03-18, release date: 2003-04-17, Last modification date: 2023-12-13)

Primary citation

Ellis, M.J.,Dodd, F.E.,Sawers, G.,Eady, R.R.,Hasnain, S.S.
Atomic Resolution Structures of Native Copper Nitrite Reductase from Alcaligenes Xylosoxidans and the Active Site Mutant Asp92Glu
J.Mol.Biol., 328:429-, 2003

PubMed Abstract: We provide the first atomic resolution (<1.20 A) structure of a copper protein, nitrite reductase, and of a mutant of the catalytically important Asp92 residue (D92E). The atomic resolution where carbon-carbon bonds of the peptide become clearly resolved, remains a key goal of structural analysis. Despite much effort and technological progress, still very few structures are known at such resolution. For example, in the Protein Data Bank (PDB) there are some 200 structures of copper proteins but the highest resolution structure is that of amicyanin, a small (12 kDa) protein, which has been resolved to 1.30 A. Here, we present the structures of wild-type copper nitrite reductase (wtNiR) from Alcaligenes xylosoxidans (36.5 kDa monomer), the "half-apo" recombinant native protein and the D92E mutant at 1.04, 1.15 and 1.12A resolutions, respectively. These structures provide the basis from which to build a detailed mechanism of this important enzyme.

PubMed: 12691751
DOI: 10.1016/S0022-2836(03)00308-5

Experimental method

X-RAY DIFFRACTION (1.04 Å)