2022
Glycerol binding at the narrow channel of photosystem II stabilizes the low-spin S2 state of the oxygen-evolving complex
Flesher DA, Liu J, Wiwczar JM, Reiss K, Yang KR, Wang J, Askerka M, Gisriel CJ, Batista VS, Brudvig GW. Glycerol binding at the narrow channel of photosystem II stabilizes the low-spin S2 state of the oxygen-evolving complex. Photosynthesis Research 2022, 152: 167-175. PMID: 35322325, PMCID: PMC9427693, DOI: 10.1007/s11120-022-00911-0.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexHydrogen bond networkS2 stateEPR signalPhotosystem II cyclesX-ray crystal structureRelative stabilityState EPR signalsD1-Asp61Water oxidationCatalytic intermediatesPhotochemical oxidationEPR spectraGlycerol moleculesCrystal structureCyanobacterial PSIIMultiline signalState SiPhotosystem IIOxidationRelative intensitiesComplexesEffect of glycerolExperimental conditionsStability
2019
Visualization of H atoms in the X‐ray crystal structure of photoactive yellow protein: Does it contain low‐barrier hydrogen bonds?
Wang J. Visualization of H atoms in the X‐ray crystal structure of photoactive yellow protein: Does it contain low‐barrier hydrogen bonds? Protein Science 2019, 28: 1966-1972. PMID: 31441173, PMCID: PMC6798185, DOI: 10.1002/pro.3716.Peer-Reviewed Original ResearchConceptsPhotoactive yellow proteinLow-barrier hydrogen bondH atomsYellow proteinResidual electron density mapsNeutron structureAtomsO bond angleO distancesO atomsHydrogen bondsElectron density mapsBond anglesDensity mapsX-ray structureCrystal structureResolution X-ray structureStructureBondsX-ray crystal structure
2014
Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix
Brown JA, Bulkley D, Wang J, Valenstein ML, Yario TA, Steitz TA, Steitz JA. Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix. Nature Structural & Molecular Biology 2014, 21: 633-640. PMID: 24952594, PMCID: PMC4096706, DOI: 10.1038/nsmb.2844.Peer-Reviewed Original Research
2010
Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand
Cortajarena AL, Wang J, Regan L. Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand. The FEBS Journal 2010, 277: 1058-1066. PMID: 20089039, DOI: 10.1111/j.1742-4658.2009.07549.x.Peer-Reviewed Original ResearchConceptsTPR domainC-terminusKey protein-protein interactionsTetratricopeptide repeat modulesChaperone heat shock proteinProtein-protein interactionsHeat shock responseHeat shock proteinsTPR proteinsChaperone functionTPR unitsProtein domainsNew packing arrangementRepeat modulesMolecular basisPeptide ligandsShock proteinsShock responseHsp90Terminal residuesX-ray crystal structureProteinCrystal structureDomainTetratricopeptide
1998
Crystal Structure Determination ofEscherichia coliClpP Starting from an EM-Derived Mask
Wang J, Hartling J, Flanagan J. Crystal Structure Determination ofEscherichia coliClpP Starting from an EM-Derived Mask. Journal Of Structural Biology 1998, 124: 151-163. PMID: 10049803, DOI: 10.1006/jsbi.1998.4058.Peer-Reviewed Original ResearchConceptsATP-dependent proteolytic complexEscherichia coli ClpPATP-dependent proteaseProteolytic active sitesEvolutionary convergenceClpP structureHeptameric ringsProteolytic complexIntracellular proteolysisProteolytic componentBiophysical techniquesClpPSmall-angle X-rayX-ray crystallographyX-ray crystal structureStriking exampleMatrix refinementActive siteProteaseStructure determinationHslVOverall architectureProteasomeStructural levelElectron microscopy