4NEX

Structure of the N-acetyltransferase domain of X. fastidiosa NAGS/K

Summary for 4NEX

• Entry DOI: 10.2210/pdb4nex/pdb
• Related: 3S6H 4K30 4NEX
• Descriptor: Acetylglutamate kinase, N-ACETYL-L-GLUTAMATE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: gcn5-related n-acetyltransferase dold, synthase, transferase
• Biological source: Xylella fastidiosa Temecula1
• Cellular location: Cytoplasm : Q87EL2
• Total number of polymer chains: 2
• Total formula weight: 39806.67

Authors

Zhao, G.,Jin, Z.,Allewell, N.M.,Tuchman, M.,Shi, D. (deposition date: 2013-10-30, release date: 2014-11-12, Last modification date: 2023-09-20)

Primary citation

Zhao, G.,Jin, Z.,Allewell, N.M.,Tuchman, M.,Shi, D.
Structures of the N-acetyltransferase domain of Xylella fastidiosaN-acetyl-L-glutamate synthase/kinase with and without a His tag bound to N-acetyl-L-glutamate.
Acta Crystallogr F Struct Biol Commun, 71:86-95, 2015

PubMed Abstract: Structures of the catalytic N-acetyltransferase (NAT) domain of the bifunctional N-acetyl-L-glutamate synthase/kinase (NAGS/K) from Xylella fastidiosa bound to N-acetyl-L-glutamate (NAG) with and without an N-terminal His tag have been solved and refined at 1.7 and 1.4 Å resolution, respectively. The NAT domain with an N-terminal His tag crystallized in space group P4(1)2(1)2, with unit-cell parameters a=b=51.72, c=242.31 Å. Two subunits form a molecular dimer in the asymmetric unit, which contains ∼41% solvent. The NAT domain without an N-terminal His tag crystallized in space group P21, with unit-cell parameters a=63.48, b=122.34, c=75.88 Å, β=107.6°. Eight subunits, which form four molecular dimers, were identified in the asymmetric unit, which contains ∼38% solvent. The structures with and without the N-terminal His tag provide an opportunity to evaluate how the His tag affects structure and function. Furthermore, multiple subunits in different packing environments allow an assessment of the plasticity of the NAG binding site, which might be relevant to substrate binding and product release. The dimeric structure of the X. fastidiosa N-acetytransferase (xfNAT) domain is very similar to that of human N-acetyltransferase (hNAT), reinforcing the notion that mammalian NAGS is evolutionally derived from bifunctional bacterial NAGS/K.

PubMed: 25615976
DOI: 10.1107/S2053230X14026788

Experimental method

X-RAY DIFFRACTION (1.6955 Å)