CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FROM FROM TETRAGONAL CRYSTALS

File:1hcm.gif


1hcm, resolution 2.5Å

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OverviewOverview

Cytochrome cd(1) nitrite reductase is a bifunctional enzyme, which can, catalyze the 1-electron reduction of nitrite to nitric oxide and the, 4-electron reduction of dioxygen to water. Here we describe the structure, of reduced nitrite reductase, crystallized under anaerobic conditions. The, structure reveals substantial domain rearrangements with the c domain, rotated by 60 degrees and shifted by approximately 20 A compared with, previously known structures from crystals grown under oxidizing, conditions. This alternative conformation gives rise to different electron, transfer routes between the c and d(1) domains and points to the, involvement of elements of very large structural changes in the function, in this enzyme. In the present structure, the c heme has a His-69/Met-106, ... [(full description)]

About this StructureAbout this Structure

1HCM is a [Single protein] structure of sequence from [Paracoccus pantotrophus] with SO4, HEC and DHE as [ligands]. Structure known Active Sites: C1A, C1B, D1A and D1B. Full crystallographic information is available from [OCA].

ReferenceReference

The Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase., Sjogren T, Hajdu J, J Biol Chem. 2001 Aug 3;276(31):29450-5. Epub 2001 May 23. PMID:11373294

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