NDLI: Structures of the N-acetyltransferase domain of Xylella fastidiosa N-acetyl-L-glutamate synthase/kinase with and without a His tag bound to N-acetyl-L-glutamate.

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Structures of the N-acetyltransferase domain of Xylella fastidiosa N-acetyl-L-glutamate synthase/kinase with and without a His tag bound to N-acetyl-L-glutamate.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zhao, Gengxiang Jin, Zhongmin Allewell, Norma M. Tuchman, Mendel Shi, Dashuang
Description	Country affiliation: United States Author Affiliation: Zhao G ( Center for Genetic Medicine Research and Department of Integrative Systems Biology, Children's National Medical Center, The George Washington University, Washington, DC 20010, USA.); Jin Z ( Southeast Regional Collaborative Access Team, Advanced Photon Source, Argonne National Laboratory, Argonne, IL 60439, USA.); Allewell NM ( Department of Cell Biology and Molecular Genetics and Department of Chemistry and Biochemistry, College of Computer, Mathematical, and Natural Sciences, University of Maryland, College Park, MD 20742, USA.); Tuchman M ( Center for Genetic Medicine Research and Department of Integrative Systems Biology, Children's National Medical Center, The George Washington University, Washington, DC 20010, USA.); Shi D ( Center for Genetic Medicine Research and Department of Integrative Systems Biology, Children's National Medical Center, The George Washington University, Washington, DC 20010, USA.)
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 1.4âÅ 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=242.31âÅ. Two subunits form a molecular dimer in the asymmetric unit, which contains â¼41% 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=75.88âÅ, ß=107.6°. Eight subunits, which form four molecular dimers, were identified in the asymmetric unit, which contains â¼38% 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.
File Format	HTM / HTML
ISSN	2053230X
DOI	10.1107/S2053230X14026788
Journal	Acta Crystallographica Section F Structural Biology Communications
Issue Number	Pt 1
Volume Number	71
Language	English
Publisher	IUCr
Publisher Date	2015-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Analytical Chemistry Bacterial Proteins Chemistry Glutamates Phosphotransferases (carboxyl Group Acceptor) Xylella Enzymology Amino Acid Sequence Catalytic Domain Crystallography, X-ray Glutamate Synthase Histidine Hydrogen Bonding Models, Molecular Oligopeptides Protein Binding Protein Structure, Quaternary Protein Structure, Secondary Structural Homology, Protein Research Support, N.i.h., Extramural Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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