2A4N

Crystal structure of aminoglycoside 6'-N-acetyltransferase complexed with coenzyme A

2A4N の概要

• エントリーDOI: 10.2210/pdb2a4n/pdb
• 関連するPDBエントリー: 1B87 1N71
• 分子名称: aac(6')-Ii, COENZYME A, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: alpha beta protein, n-acetyl transferase, transferase
• 由来する生物種: Enterococcus faecium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43187.58

構造登録者

Burk, D.L.,Xiong, B.,Breitbach, C.,Berghuis, A.M. (登録日: 2005-06-29, 公開日: 2005-09-20, 最終更新日: 2023-08-23)

主引用文献

Burk, D.L.,Xiong, B.,Breitbach, C.,Berghuis, A.M.
Structures of aminoglycoside acetyltransferase AAC(6')-Ii in a novel crystal form: structural and normal-mode analyses.
Acta Crystallogr.,Sect.D, 61:1273-1279, 2005

PubMed Abstract: The aminoglycoside-modifying enzyme aminoglycoside 6'-N-acetyltransferase type Ii [AAC(6')-Ii] has been crystallized with its cofactor coenzyme A in space group C222(1), with unit-cell parameters a = 71.5, b = 127.4, c = 76.9 A and one physiologically relevant dimer species per asymmetric unit. The space group previously observed for this complex was P2(1)2(1)2(1), with two dimers per asymmetric unit. By comparing the six available protomer structures of the AAC(6')-Ii-CoA complex, it has been possible to identify regions of plasticity within the protein. Normal-mode analysis of this complex suggests that this plasticity is not an artefact of crystal-packing forces, but that the region of the protomer that displays multiple conformations is intrinsically flexible. It is conjectured that the flexibility is relevant for the cooperative activity observed for the enzyme.

PubMed: 16131761
DOI: 10.1107/S0907444905021487

実験手法

X-RAY DIFFRACTION (2.2 Å)