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  X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase

Lai, J., Niks, D., Wang, Y., Domratcheva, T., Barends, T., Schwarz, F., et al. (2011). X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase. Journal of the American Chemical Society, 133(1), 4-7. doi:10.1021/ja106555c.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-1350-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-1351-D
Genre: Journal Article
Alternative Title : X-ray and NMR crystallography in an enzyme active site: the indoline quinonoid intermediate in tryptophan synthase

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 Creators:
Lai, J., Author
Niks, Dimitri, Author
Wang, Yichun, Author
Domratcheva, Tatiana1, Author              
Barends, Thomas1, Author              
Schwarz, Friedrich1, Author              
Olsen, R. A., Author
Elliott, D. W., Author
Fatmi, M. Q., Author
Chang, C. A., Author
Schlichting, Ilme1, Author              
Dunn, Michael F., Author
Mueller, L., Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Chemical−level details such as protonation and hybridization state are critical for understanding enzyme mechanism and function. Even at high resolution, these details are difficult to determine by X−ray crystallography alone. The chemical shift in NMR spectroscopy, however, is an extremely sensitive probe of the chemical environment, making solid−state NMR spectroscopy and X−ray crystallography a powerful combination for defining chemically detailed three−dimensional structures. Here we adopted this combined approach to determine the chemically rich crystal structure of the indoline quinonoid intermediate in the pyridoxal−5'−phosphate−dependent enzyme tryptophan synthase under conditions of active catalysis. Models of the active site were developed using a synergistic approach in which the structure of this reactive substrate analogue was optimized using ab initio computational chemistry in the presence of side−chain residues fixed at their crystallographically determined coordinates. Various models of charge and protonation state for the substrate and nearby catalytic residues could be uniquely distinguished by their calculated effects on the chemical shifts measured at specifically 13C− and 15N−labeled positions on the substrate. Our model suggests the importance of an equilibrium between tautomeric forms of the substrate, with the protonation state of the major isomer directing the next catalytic step

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Language(s): eng - English
 Dates: 2010-07-232011-01-12
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 664537
DOI: 10.1021/ja106555c
Other: 7651
 Degree: -

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Title: Journal of the American Chemical Society
  Other : J. Am. Chem. Soc.
  Abbreviation : JACS
Source Genre: Journal
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Publ. Info: American Chemical Society
Pages: - Volume / Issue: 133 (1) Sequence Number: - Start / End Page: 4 - 7 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870