1A8C

PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERROCYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITHOUT HYDROGEN BOND CONSTRAINTS

1A8C の概要

• エントリーDOI: 10.2210/pdb1a8c/pdb
• 分子名称: FERROCYTOCHROME C-552, HEME C (2 entities in total)
• 機能のキーワード: hemoprotein, cytochrome, prokaryotic electron transport
• 由来する生物種: Nitrosomonas europaea
• 細胞内の位置: Periplasm: P95339
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9110.20

構造登録者

Timkovich, R.,Bergmann, D.,Arciero, D.M.,Hooper, A.B. (登録日: 1998-03-23, 公開日: 1998-10-21, 最終更新日: 2024-10-30)

主引用文献

Timkovich, R.,Bergmann, D.,Arciero, D.M.,Hooper, A.B.
Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea.
Biophys.J., 75:1964-1972, 1998

PubMed Abstract: 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.

PubMed: 9746537

実験手法

SOLUTION NMR