4AVA

Crystal structure of protein lysine acetyltransferase Rv0998 from Mycobacterium tuberculosis

4AVA の概要

• エントリーDOI: 10.2210/pdb4ava/pdb
• 関連するPDBエントリー: 4AVB 4AVC
• 分子名称: LYSINE ACETYLTRANSFERASE, ACETYL COENZYME *A, ACETATE ION, ... (7 entities in total)
• 機能のキーワード: transferase, allosteric regulation, domain coupling
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37015.16

構造登録者

Lee, H.J.,Lang, P.T.,Fortune, S.M.,Sassetti, C.M.,Alber, T. (登録日: 2012-05-24, 公開日: 2012-07-11, 最終更新日: 2024-05-08)

主引用文献

Lee, H.J.,Lang, P.T.,Fortune, S.M.,Sassetti, C.M.,Alber, T.
Cyclic AMP Regulation of Protein Lysine Acetylation in Mycobacterium Tuberculosis.
Nat.Struct.Mol.Biol., 19:811-, 2012

PubMed Abstract: Protein lysine acetylation networks can regulate central processes such as carbon metabolism and gene expression in bacteria. In Escherichia coli, cyclic AMP (cAMP) regulates protein lysine acetyltransferase (PAT) activity at the transcriptional level, but in Mycobacterium tuberculosis, fusion of a cyclic nucleotide-binding domain to a Gcn5-like PAT domain enables direct cAMP control of protein acetylation. Here we describe the allosteric activation mechanism of M. tuberculosis PAT. The crystal structures of the autoinhibited and cAMP-activated PAT reveal that cAMP binds to a cryptic site in the regulatory domain that is over 32 Å from the catalytic site. An extensive conformational rearrangement relieves this autoinhibition by means of a substrate-mimicking lid that covers the protein-substrate binding surface. A steric double latch couples the domains by harnessing a classic, cAMP-mediated conformational switch. The structures suggest general features that enable the evolution of long-range communication between linked domains.

PubMed: 22773105
DOI: 10.1038/NSMB.2318

実験手法

X-RAY DIFFRACTION (1.698 Å)