STRUCTURE OF ALCALIGENES FAECALIS NITRITE REDUCTASE AND A COPPER SITE MUTANT, M150E, THAT CONTAINS ZINC

File:2afn.gif


2afn, resolution 2.0Å

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OverviewOverview

The structures at 2.0 and 2.25 A resolution of native and recombinant, nitrite reductase from Alcaligenes faecalis show that they are identical, to each other and very similar to nitrite reductase from Achromobacter, cycloclastes. The crystallographic structure of a mutant, M150E, which, unlike the wild-type protein cannot be reduced by pseudoazurin, shows that, the glutamate replacement for methionine binds to a metal at the type I Cu, site via only one oxygen. Anomalous scattering data collected at, wavelengths of 1.040 and 1.377 A reveal that the metal at the type I site, is a Zn. No significant differences from the native structure other than, local perturbations at the type I site are seen. A local pseudo 2-fold, axis relates the two domains of different monomers which form the ... [(full description)]

About this StructureAbout this Structure

2AFN is a [Single protein] structure of sequence from [Alcaligenes faecalis] with CU as [ligand]. This structure superseeds the now removed PDB entry 1AFN. Active as [Transferred entry: 1.7.2.1], with EC number [1.7.99.3]. Structure known Active Sites: CU1, CU2, CU3, CU4, CU5 and CU6. Full crystallographic information is available from [OCA].

ReferenceReference

Structure of Alcaligenes faecalis nitrite reductase and a copper site mutant, M150E, that contains zinc., Murphy ME, Turley S, Kukimoto M, Nishiyama M, Horinouchi S, Sasaki H, Tanokura M, Adman ET, Biochemistry. 1995 Sep 26;34(38):12107-17. PMID:7547950

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