4ORF

cAMP-binding acyltransferase from Mycobacterium smegmatis, mutant R95K

4ORF の概要

• エントリーDOI: 10.2210/pdb4orf/pdb
• 関連するPDBエントリー: 4OLL 4ONU
• 分子名称: Acetyltransferase Pat, CHLORIDE ION (3 entities in total)
• 機能のキーワード: alpha-beta fold, linker peptide, cyclic nucleotide binding domain, acyl-transferase domain, transferase
• 由来する生物種: Mycobacterium smegmatis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37574.41

構造登録者

Podobnik, M.,Rebolj, K.,Visweswariah, S.S. (登録日: 2014-02-11, 公開日: 2014-04-30, 最終更新日: 2024-02-28)

主引用文献

Podobnik, M.,Siddiqui, N.,Rebolj, K.,Nambi, S.,Merzel, F.,Visweswariah, S.S.
Allostery and Conformational Dynamics in cAMP-binding Acyltransferases.
J.Biol.Chem., 289:16588-16600, 2014

PubMed Abstract: Mycobacteria harbor unique proteins that regulate protein lysine acylation in a cAMP-regulated manner. These lysine acyltransferases from Mycobacterium smegmatis (KATms) and Mycobacterium tuberculosis (KATmt) show distinctive biochemical properties in terms of cAMP binding affinity to the N-terminal cyclic nucleotide binding domain and allosteric activation of the C-terminal acyltransferase domain. Here we provide evidence for structural features in KATms that account for high affinity cAMP binding and elevated acyltransferase activity in the absence of cAMP. Structure-guided mutational analysis converted KATms from a cAMP-regulated to a cAMP-dependent acyltransferase and identified a unique asparagine residue in the acyltransferase domain of KATms that assists in the enzymatic reaction in the absence of a highly conserved glutamate residue seen in Gcn5-related N-acetyltransferase-like acyltransferases. Thus, we have identified mechanisms by which properties of similar proteins have diverged in two species of mycobacteria by modifications in amino acid sequence, which can dramatically alter the abundance of conformational states adopted by a protein.

PubMed: 24748621
DOI: 10.1074/jbc.M114.560086

実験手法

X-RAY DIFFRACTION (2 Å)