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Neutron diffraction...
Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase
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- Drago, Victoria N. (författare)
- University of Toledo,Oak Ridge National Laboratory
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- Devos, Juliette M. (författare)
- Institut Laue Langevin
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- Blakeley, Matthew P. (författare)
- Institut Laue Langevin
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- Forsyth, V. Trevor (författare)
- Lund University,Lunds universitet,LINXS - Institute of advanced Neutron and X-ray Science,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Molekylär Biofysik,Forskargrupper vid Lunds universitet,LU profilområde: Proaktivt åldrande,Lunds universitets profilområden,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Molecular Biophysics,Lund University Research Groups,LU Profile Area: Proactive Ageing,Lund University Profile areas
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- Parks, Jerry M. (författare)
- Oak Ridge National Laboratory
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- Kovalevsky, Andrey (författare)
- Oak Ridge National Laboratory
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- Mueser, Timothy C. (författare)
- University of Toledo
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(creator_code:org_t)
- 2024
- 2024
- Engelska.
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Ingår i: Cell Reports Physical Science. - 2666-3864. ; 5:2
- Relaterad länk:
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http://dx.doi.org/10... (free)
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https://lup.lub.lu.s...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Pyridoxal 5′-phosphate (PLP), the biologically active form of vitamin B6, is an essential cofactor in many biosynthetic pathways. The emergence of PLP-dependent enzymes as drug targets and biocatalysts, such as tryptophan synthase (TS), has underlined the demand to understand PLP-dependent catalysis and reaction specificity. The ability of neutron diffraction to resolve the positions of hydrogen atoms makes it an ideal technique to understand how the electrostatic environment and selective protonation of PLP regulates PLP-dependent activities. Facilitated by microgravity crystallization of TS with the Toledo Crystallization Box, we report the 2.1 Å joint X-ray/neutron (XN) structure of TS with PLP in the internal aldimine form. Positions of hydrogens were directly determined in both the α- and β-active sites, including PLP cofactor. The joint XN structure thus provides insight into the selective protonation of the internal aldimine and the electrostatic environment of TS necessary to understand the overall catalytic mechanism.
Ämnesord
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
Nyckelord
- enzyme mechanism
- fold-type II
- macromolecular crystallography
- microgravity crystallization
- neutron crystallography
- neutron diffraction
- pyridoxal 5’-phosphate
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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