0000000000179747

AUTHOR

Miguel López-estepa

showing 3 related works from this author

Elucidating the catalytic reaction mechanism of orotate phosphoribosyltransferase by means of X-ray crystallography and computational simulations

2020

15 p.-8 fig.-2 tab.1 graph. abst.+ 8 fig. supl.-1 tab. supl.

PyrimidineStereochemistry010402 general chemistry01 natural sciencesCatalysisEnzyme catalysischemistry.chemical_compoundOrotidineNucleotideReaction mechanismchemistry.chemical_classificationMD simulations010405 organic chemistryHydrogen bondEnzyme catalysisGeneral ChemistryTautomer0104 chemical sciencesPyrimidine metabolismOrotate phosphoribosyltransferasechemistryPyrimidine metabolismOrotate phosphoribosyltransferaseQM/MM methodsX-ray structure
researchProduct

Mechanism of sulfur transfer across protein-protein interfaces: The cysteine desulfurase model system

2016

CsdA cysteine desulfurase (the sulfur donor) and the CsdE sulfur acceptor are involved in biological sulfur trafficking and in iron-sulfur cluster assembly in the model bacterium Escherichia coli. CsdA and CsdE form a stable complex through a polar interface that includes CsdA Cys328 and CsdE Cys61, the two residues known to be involved in the sulfur transfer reaction. Although mechanisms for the transfer of a sulfur moiety across protein-protein interfaces have been proposed based on the IscS-IscU and IscS-TusA structures, the flexibility of the catalytic cysteine loops involved has precluded a high resolution view of the active-site geometry and chemical environment for sulfur transfer. H…

inorganic chemicals0301 basic medicineChemistryCysteine desulfuraseInorganic chemistrychemistry.chemical_elementIsothermal titration calorimetryGeneral Chemistry010402 general chemistry01 natural sciencesCombinatorial chemistryAcceptorSulfurCatalysis0104 chemical sciences03 medical and health sciences030104 developmental biologyMoietyTransferaseBiogenesisCysteine
researchProduct

Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE

2017

17 p.-8 fig.

0301 basic medicineProtein ConformationDimerlcsh:MedicineMolecular DynamicsCrystallography X-RayPhysical ChemistryBiochemistryDEAD-box RNA HelicasesMolecular dynamicschemistry.chemical_compoundComputational ChemistryNucleophileBiochemical Simulationslcsh:ScienceMultidisciplinaryCrystallographyChemistryOrganic CompoundsPhysicsEscherichia coli ProteinsCondensed Matter Physics3. Good healthPhysical sciencesChemistryCarbon-Sulfur LyasesBiochemistryCrystal StructureResearch ArticleChemical ElementsProtein subunitChemical physicschemistry.chemical_elementOxidative phosphorylationMolecular Dynamics Simulation03 medical and health sciencesThiolsEscherichia coliSolid State PhysicsProtein Interaction Domains and MotifsChemical BondingOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesComputational BiologyDimers (Chemical physics)Hydrogen BondingCell BiologySulfurAcceptorRedox sensitiveOxidative Stress030104 developmental biologyBiophysicslcsh:QProtein MultimerizationSulfur
researchProduct