1QLK

SOLUTION STRUCTURE OF CA(2+)-LOADED RAT S100B (BETABETA) NMR, 20 STRUCTURES

1QLK の概要

• エントリーDOI: 10.2210/pdb1qlk/pdb
• NMR情報: BMRB: 5544
• 分子名称: S-100 PROTEIN, CALCIUM ION (2 entities in total)
• 機能のキーワード: s100beta, s100b, ef-hand, s100 protein, calcium-binding protein, four-helix bundle, calcium-binding
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm (By similarity): P04631
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21676.41

構造登録者

Drohat, A.C.,Baldisseri, D.M.,Rustandi, R.R.,Weber, D.J. (登録日: 1997-09-26, 公開日: 1998-11-11, 最終更新日: 2024-05-22)

主引用文献

Drohat, A.C.,Baldisseri, D.M.,Rustandi, R.R.,Weber, D.J.
Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,.
Biochemistry, 37:2729-2740, 1998

PubMed Abstract: The three-dimensional structure of Ca2+-bound rat S100B(betabeta) has been determined using data from a series of two-dimensional (2D), three-dimensional (3D), and four-dimensional (4D) nuclear magnetic resonance (NMR) experiments. Each S100beta subunit (91 residues) contains four helixes (helix 1, E2-R20; helix 2, K29-N38; helix 3, Q50-D61; and helix 4, F70-A83) and one antiparallel beta-sheet (strand 1, K26-K28; and strand 2, E67-D69) which brings the normal and pseudo EF-hands together. As found previously for rat apo-S100B(betabeta) [Drohat, A. C., et al. (1996) Biochemistry 35, 11577-11588], helixes 1, 1', 4, and 4' associate to form an X-type four-helix bundle at the symmetric dimer interface. Additionally, Ca2+ binding does not significantly change the interhelical angle of helixes 1 and 2 in the pseudo EF-hand (apo, Omega1-2 = 132 +/- 4 degrees; and Ca2+-bound, Omega1-2 = 137 +/- 5 degrees). However, the interhelical angle of helixes 3 and 4 in the normal EF-hand (Omega3-4 = 106 +/- 4 degrees) changed significantly upon the addition of Ca2+ (DeltaOmega3-4 = 112 +/- 5 degrees) and is similar to that of the Ca2+-bound EF-hands in calbindin D9K, calmodulin, and troponin (84 degrees PubMed: 9485423
DOI: 10.1021/bi972635p

実験手法

SOLUTION NMR