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	Temperature-Resolved Cryo-EM Uncovers Structural Bases of Temperature-Dependent Enzyme Functions.
Journal, issue, pages	J Am Chem Soc, Vol. 141, Issue 51, Page 19983-19987, Year 2019
Publish date	Dec 26, 2019
Authors	Chin-Yu Chen / Yuan-Chih Chang / Bo-Lin Lin / Chun-Hsiang Huang / Ming-Daw Tsai /
PubMed Abstract	Protein functions are temperature-dependent, but protein structures are usually solved at a single (often low) temperature because of limitations on the conditions of crystal growth or protein ...Protein functions are temperature-dependent, but protein structures are usually solved at a single (often low) temperature because of limitations on the conditions of crystal growth or protein vitrification. Here we demonstrate the feasibility of solving cryo-EM structures of proteins vitrified at high temperatures, solve 12 structures of an archaeal ketol-acid reductoisomerase (KARI) vitrified at 4-70 °C, and show that structures of both the Mg form (KARI:2Mg) and its ternary complex (KARI:2Mg:NADH:inhibitor) are temperature-dependent in correlation with the temperature dependence of enzyme activity. Furthermore, structural analyses led to dissection of the induced-fit mechanism into ligand-induced and temperature-induced effects and to capture of temperature-resolved intermediates of the temperature-induced conformational change. The results also suggest that it is preferable to solve cryo-EM structures of protein complexes at functional temperatures. These studies should greatly expand the landscapes of protein structure-function relationships and enhance the mechanistic analysis of enzymatic functions.
External links	J Am Chem Soc / PubMed:31829582
Methods	EM (single particle)
Resolution	2.17 - 3.0 Å
Structure data	0740 6kou EMDB-0740, PDB-6kou: 277 K cryoEM structure of Sso-KARI in complex with magnesium ions Method: EM (single particle) / Resolution: 2.43 Å 0742 6kpa EMDB-0742, PDB-6kpa: 277 K cryoEM structure of Sso-KARI in complex with Mg2+, NADH and CPD Method: EM (single particle) / Resolution: 2.75 Å 0743 6kpe EMDB-0743, PDB-6kpe: 343 K cryoEM structure of Sso-KARI in complex with Mg2+ Method: EM (single particle) / Resolution: 2.83 Å 0746 6kph EMDB-0746, PDB-6kph: 343 K cryoEM structure of Sso-KARI in complex with Mg2+, NADH and CPD Method: EM (single particle) / Resolution: 2.41 Å 0747 6kpi EMDB-0747, PDB-6kpi: 298 K cryoEM structure of Sso-KARI in complex with Mg2+ Method: EM (single particle) / Resolution: 2.43 Å 0748 6kpj EMDB-0748, PDB-6kpj: 298 K cryoEM structure of Sso-KARI in complex with Mg2+, NADH and CPD Method: EM (single particle) / Resolution: 2.56 Å 0749 6kpk EMDB-0749, PDB-6kpk: 309 K cryoEM structure of Sso-KARI in complex with Mg2+ Method: EM (single particle) / Resolution: 2.3 Å 0750 6kq4 EMDB-0750, PDB-6kq4: 323 K cryoEM structure of Sso-KARI in complex with Mg2+ Method: EM (single particle) / Resolution: 2.3 Å 0751 6kq8 EMDB-0751, PDB-6kq8: 328 K cryoEM structure of Sso-KARI in complex with Mg2+ Method: EM (single particle) / Resolution: 3.0 Å 0752 6kqj EMDB-0752, PDB-6kqj: 309 K cryoEM structure of Sso-KARI in complex with Mg2+, NADH and CPD Method: EM (single particle) / Resolution: 2.54 Å 0753 6kqk EMDB-0753, PDB-6kqk: 323 K cryoEM structure of Sso-KARI in complex with Mg2+, NADH and CPD Method: EM (single particle) / Resolution: 2.17 Å 0754 6kqo EMDB-0754, PDB-6kqo: 328 K cryoEM structure of Sso-KARI in complex with Mg2+, NADH and CPD Method: EM (single particle) / Resolution: 2.52 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-NAI: 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE ChemComp-9TY: cyclopropane-1,1-dicarboxylic acid
Source	saccharolobus solfataricus (archaea)
Keywords	ISOMERASE / Complex