2A4N

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

Summary for 2A4N

• Entry DOI: 10.2210/pdb2a4n/pdb
• Related: 1B87 1N71
• Descriptor: aac(6')-Ii, COENZYME A, SULFATE ION, ... (4 entities in total)
• Functional Keywords: alpha beta protein, n-acetyl transferase, transferase
• Biological source: Enterococcus faecium
• Total number of polymer chains: 2
• Total formula weight: 43187.58

Authors

Burk, D.L.,Xiong, B.,Breitbach, C.,Berghuis, A.M. (deposition date: 2005-06-29, release date: 2005-09-20, Last modification date: 2023-08-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)