3QPI

Crystal Structure of Dimeric Chlorite Dismutases from Nitrobacter winogradskyi

Summary for 3QPI

• Entry DOI: 10.2210/pdb3qpi/pdb
• Descriptor: Chlorite Dismutase, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: oxygen, oxidoreductase, chlorite o(2)-lyase, cytoplasma, chlorite
• Biological source: Nitrobacter winogradskyi
• Total number of polymer chains: 2
• Total formula weight: 43721.02

Authors

Mlynek, G.,Sjoeblom, B.,Kostan, J.,Fuereder, S.,Maixner, F.,Furtmueller, P.G.,Obinger, O.,Wagner, M.,Daims, H.,Djinovic-Carugo, K. (deposition date: 2011-02-13, release date: 2011-07-06, Last modification date: 2024-02-21)

Primary citation

Mlynek, G.,Sjoblom, B.,Kostan, J.,Fureder, S.,Maixner, F.,Gysel, K.,Furtmuller, P.G.,Obinger, C.,Wagner, M.,Daims, H.,Djinovic-Carugo, K.
Unexpected diversity of chlorite dismutases: a catalytically efficient dimeric enzyme from Nitrobacter winogradskyi.
J.Bacteriol., 193:2408-2417, 2011

PubMed Abstract: Chlorite dismutase (Cld) is a unique heme enzyme catalyzing the conversion of ClO(2)(-) to Cl(-) and O(2). Cld is usually found in perchlorate- or chlorate-reducing bacteria but was also recently identified in a nitrite-oxidizing bacterium of the genus Nitrospira. Here we characterized a novel Cld-like protein from the chemolithoautotrophic nitrite oxidizer Nitrobacter winogradskyi which is significantly smaller than all previously known chlorite dismutases. Its three-dimensional (3D) crystal structure revealed a dimer of two identical subunits, which sharply contrasts with the penta- or hexameric structures of other chlorite dismutases. Despite a truncated N-terminal domain in each subunit, this novel enzyme turned out to be a highly efficient chlorite dismutase (K(m) = 90 μM; k(cat) = 190 s(-1); k(cat)/K(m) = 2.1 × 10(6) M(-1) s(-1)), demonstrating a greater structural and phylogenetic diversity of these enzymes than was previously known. Based on comparative analyses of Cld sequences and 3D structures, signature amino acid residues that can be employed to assess whether uncharacterized Cld-like proteins may have a high chlorite-dismutating activity were identified. Interestingly, proteins that contain all these signatures and are phylogenetically closely related to the novel-type Cld of N. winogradskyi exist in a large number of other microbes, including other nitrite oxidizers.

PubMed: 21441524
DOI: 10.1128/JB.01262-10

Experimental method

X-RAY DIFFRACTION (2.1 Å)