3CLP

M. loti cyclic-nucleotide binding domain mutant 2

3CLP の概要

• エントリーDOI: 10.2210/pdb3clp/pdb
• 関連するPDBエントリー: 1VP6 1u12 3BEH 3CL1 3CO2
• 分子名称: Mll3241 protein, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: mlotik1 cyclic-nucleotide binding domain mutant 2. cyclic-amp bound, membrane protein
• 由来する生物種: RHIZOBIUM LOTI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30280.44

構造登録者

Clayton, G.M.,Altieri, S.L.,Thomas, L.R.,Morais-Cabral, J.H. (登録日: 2008-03-19, 公開日: 2008-08-05, 最終更新日: 2024-02-21)

主引用文献

Altieri, S.L.,Clayton, G.M.,Silverman, W.R.,Olivares, A.O.,De La Cruz, E.M.,Thomas, L.R.,Morais-Cabral, J.H.
Structural and Energetic Analysis of Activation by a Cyclic Nucleotide Binding Domain.
J.Mol.Biol., 381:655-669, 2008

PubMed Abstract: MlotiK1 is a prokaryotic homolog of cyclic-nucleotide-dependent ion channels that contains an intracellular C-terminal cyclic nucleotide binding (CNB) domain. X-ray structures of the CNB domain have been solved in the absence of ligand and bound to cAMP. Both the full-length channel and CNB domain fragment are easily expressed and purified, making MlotiK1 a useful model system for dissecting activation by ligand binding. We have used X-ray crystallography to determine three new MlotiK1 CNB domain structures: a second apo configuration, a cGMP-bound structure, and a second cAMP-bound structure. In combination, the five MlotiK1 CNB domain structures provide a unique opportunity for analyzing, within a single protein, the structural differences between the apo state and the bound state, and the structural variability within each state. With this analysis as a guide, we have probed the nucleotide selectivity and importance of specific residue side chains in ligand binding and channel activation. These data help to identify ligand-protein interactions that are important for ligand dependence in MlotiK1 and, more globally, in the class of nucleotide-dependent proteins.

PubMed: 18619611
DOI: 10.1016/j.jmb.2008.06.011

実験手法

X-RAY DIFFRACTION (2 Å)