NMR assignments of cd-HO, a 24 kDa heme oxygenase from Corynebacterium diphtheria.
We are employing a number of selective in vitro and in vivo methods including NMR to screen compounds that bind to heme oxygenases from pathogenic bacteria. We report the nearly complete HN, N, CO, Calpha and Cbeta chemical shift assignments of a 215-amino acid HO from Corynebacterium diphtheria in three forms, apo cd-HO-G135A, apo cd-HO and CO-bound ferrous holo cd-HO; these assignments will enable us to identify residues on cd-HO that are perturbed upon binding to selected compounds, and to help with the development of inhibitors specific to the bacterial proteins.
Hom
Kellie
K
Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, 20 Penn Street, Baltimore, MD 21201, USA.
Furci
Lena M
LM
Deshmukh
Rahul
R
Wilks
Angela
A
D001051:Apoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003353:Corynebacterium diphtheriae / Q000201:enzymology* / Q000235:genetics; D006419:Heme Oxygenase (Decyclizing) / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020035:Holoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D001051:Apoenzymes; D001426:Bacterial Proteins; D020035:Holoenzymes; D011994:Recombinant Proteins; D006419:Heme Oxygenase (Decyclizing)