Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Substrate specificity of plant nitrilase complexes is affected by their helical twist.
Journal, issue, pages	Commun Biol, Vol. 1, Page 186, Year 2018
Publish date	Nov 2, 2018
Authors	Jeremy D Woodward / Inga Trompetter / B Trevor Sewell / Markus Piotrowski /
PubMed Abstract	Nitrilases are oligomeric, helix-forming enzymes from plants, fungi and bacteria that are involved in the metabolism of various natural and artificial nitriles. These biotechnologically important ...Nitrilases are oligomeric, helix-forming enzymes from plants, fungi and bacteria that are involved in the metabolism of various natural and artificial nitriles. These biotechnologically important enzymes are often specific for certain substrates, but directed attempts at modifying their substrate specificities by exchanging binding pocket residues have been largely unsuccessful. Thus, the basis for their selectivity is still unknown. Here we show, based on work with two highly similar nitrilases from the plant , that modifying nitrilase helical twist, either by exchanging an interface residue or by imposing a different twist, without altering any binding pocket residues, changes substrate preference. We reveal that helical twist and substrate size correlate and when binding pocket residues are exchanged between two nitrilases that show the same twist but different specificities, their specificities change. Based on these findings we propose that helical twist influences the overall size of the binding pocket.
External links	Commun Biol / PubMed:30417123 / PubMed Central
Methods	EM (helical sym.)
Resolution	20.0 Å
Structure data	EMDB-3486: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3496: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3497: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3498: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3499: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3500: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3501: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3503: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3504: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å EMDB-3505: Substrate specificity in plant nitrilase helical assemblies is determined by their twist. Method: EM (helical sym.) / Resolution: 20.0 Å
Source	Arabidopsis thaliana (thale cress) Caenorhabditis elegans (invertebrata) Capsella rubella (plant) Lotus japonicus (plant) Sinapis alba (white mustard)