1DEG

THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE

1DEG の概要

• エントリーDOI: 10.2210/pdb1deg/pdb
• 分子名称: CALMODULIN, CALCIUM ION (2 entities in total)
• 機能のキーワード: calcium-binding protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cytoplasm, cytoskeleton, spindle: P02593
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16194.93

構造登録者

Raghunathan, S.,Chandross, R.,Cheng, B.P.,Persechini, A.,Sobottk, S.E.,Kretsinger, R.H. (登録日: 1993-06-07, 公開日: 1994-05-31, 最終更新日: 2024-02-07)

主引用文献

Raghunathan, S.,Chandross, R.J.,Cheng, B.P.,Persechini, A.,Sobottka, S.E.,Kretsinger, R.H.
The linker of des-Glu84-calmodulin is bent.
Proc.Natl.Acad.Sci.Usa, 90:6869-6873, 1993

PubMed Abstract: The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand domains 1 and 2 (lobe 1,2) do not touch lobe 3,4. The length, by alpha-carbon separation, of des-Glu84-CaM is 56 A; that of native CaM is 64 A. The shape of des-Glu84-CaM is similar to that of native CaM, as it is bound to the target peptide of myosin light-chain kinase. This result supports the proposal that the linker region of the central helix of CaM functions as a flexible tether.

PubMed: 8341712
DOI: 10.1073/pnas.90.14.6869

実験手法

X-RAY DIFFRACTION (2.9 Å)