1IKU

myristoylated recoverin in the calcium-free state, NMR, 22 structures

1IKU の概要

• エントリーDOI: 10.2210/pdb1iku/pdb
• 分子名称: RECOVERIN, MYRISTIC ACID (2 entities in total)
• 機能のキーワード: calcium-myristoyl switch, calcuim-binding protein, calcium-binding protein
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23463.58

構造登録者

Tanaka, T.,Ames, J.B.,Harvey, T.S.,Stryer, L.,Ikura, M. (登録日: 1996-01-18, 公開日: 1996-07-11, 最終更新日: 2024-11-13)

主引用文献

Tanaka, T.,Ames, J.B.,Harvey, T.S.,Stryer, L.,Ikura, M.
Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state.
Nature, 376:444-447, 1995

PubMed Abstract: Recoverin, a retinal calcium-binding protein of relative molecular mass (M(r)) 23K, participates in the recovery phase of visual excitation and in adaptation to background light. The Ca(2+)-bound form of recoverin prolongs the photoresponse, probably by blocking phosphorylation of photoexcited rhodopsin. Retinal recoverin contains a covalently attached myristoyl group or related acyl group at its amino terminus and two Ca(2+)-binding sites. Ca2+ binding to myristoylated, but not unmyristoylated, recoverin induces its translocation to bilayer membranes, indicating that the myristoyl group is essential to the read-out of calcium signals (calcium-myristoyl switch). Here we present the solution structure of Ca(2+)-free, myristoylated recombinant recoverin obtained by heteronuclear multidimensional NMR spectroscopy. The myristoyl group is sequestered in a deep hydrophobic pocket formed by many aromatic and other hydrophobic residues from five flanking helices.

PubMed: 7630423
DOI: 10.1038/376444a0

実験手法

SOLUTION NMR