1a56
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PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERRICYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITH EXPLICIT HYDROGEN BOND CONSTRAINTS
OverviewOverview
Cytochrome c-552 from Nitrosomonas europaea is a 9.1-kDa monoheme protein, that is a member of the bacterial cytochrome c-551 family. The gene, encoding for c-552 has been cloned and sequenced and the primary sequence, of the product deduced. Proton resonance assignments were made for all, main-chain and most side-chain protons in the diamagnetic, reduced form by, two-dimensional NMR techniques. Distance constraints (1056) were, determined from nuclear Overhauser enhancements, and torsion angle, constraints (88) were determined from scalar coupling estimates. Solution, conformations for the protein were computed by the hybrid distance, geometry-simulated annealing approach. For 20 computed structures, the, root mean squared deviation from the average position of equivalent atoms, was 0.84 A (sigma = 0.12) for backbone atoms over all residues. Analysis, by residue revealed there were three regions clearly less well defined, than the rest of the protein: the first two residues at the N-terminus, the last two at the C-terminus, and a loop region from residues 34 to 40., Omitting these regions from the comparison, the root mean squared, deviation was 0.61 A (sigma = 0.13) for backbone atoms, 0.86 A (sigma =, 0.12) for all associated heavy atoms, and 0. 43 A (sigma = 0.17) for the, heme group. The global folding of the protein is consistent with others in, the c-551 family. A deletion at the N-terminus relative to other family, members had no impact on the global folding, whereas an insertion at, residue 65 did affect the way the polypeptide packs against the, methionine-ligated side of the heme. The effects of specific substitutions, will be discussed. The structure of c-552 serves to delineate essential, features of the c-551 family.
About this StructureAbout this Structure
1A56 is a Single protein structure of sequence from Nitrosomonas europaea with HEC as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea., Timkovich R, Bergmann D, Arciero DM, Hooper AB, Biophys J. 1998 Oct;75(4):1964-72. PMID:9746537
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