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4AVC

Crystal structure of protein lysine acetyltransferase Rv0998 in complex with acetyl CoA and cAMP

4AVC の概要
エントリーDOI10.2210/pdb4avc/pdb
関連するPDBエントリー4AVA 4AVB
分子名称LYSINE ACETYLTRANSFERASE, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE, ACETYL COENZYME *A, ... (6 entities in total)
機能のキーワードtransferase, acetyltransferase, allosteric regulation, domain coupling
由来する生物種MYCOBACTERIUM TUBERCULOSIS
タンパク質・核酸の鎖数2
化学式量合計75106.90
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: 2024-11-13)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.806 Å)
構造検証レポート
Validation report summary of 4avc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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