1HRQ

THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR

1HRQ の概要

• エントリーDOI: 10.2210/pdb1hrq/pdb
• 分子名称: HIGH POTENTIAL IRON SULFUR PROTEIN, IRON/SULFUR CLUSTER (2 entities in total)
• 機能のキーワード: electron transfer (iron-sulfur protein)
• 由来する生物種: Allochromatium vinosum
• 細胞内の位置: Periplasm: P00260
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9264.57

構造登録者

Banci, L.,Bertini, I.,Dikiy, A.,Kastrau, D.H.W.,Luchinat, C.,Sompornpisut, P. (登録日: 1995-01-17, 公開日: 1995-06-03, 最終更新日: 2024-05-22)

主引用文献

Banci, L.,Bertini, I.,Dikiy, A.,Kastrau, D.H.,Luchinat, C.,Sompornpisut, P.
The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.
Biochemistry, 34:206-219, 1995

PubMed Abstract: The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., & Wemmer, D. E. (1992) Biochemistry 31, 5632-5639] has been extended up to 85% of the total protein protons. Ninety percent of the nitrogens have been assigned. Then the solution structure has been obtained using as many as 1147 meaningful NOE connectivities. The protein is sizably paramagnetic even though the ground state is a singlet. Nevertheless, the final RMSD values are 0.62 and 1.19 A for the backbone and the heavy atoms, respectively. These values compare well with those for diamagnetic proteins of the same size. The solution structure is discussed in the light of the available structural information from X-ray data.

PubMed: 7819198
DOI: 10.1021/bi00001a025

実験手法

SOLUTION NMR