2019
Crystal structures of p120RasGAP N-terminal SH2 domain in its apo form and in complex with a p190RhoGAP phosphotyrosine peptide
Chehayeb R, Stiegler AL, Boggon TJ. Crystal structures of p120RasGAP N-terminal SH2 domain in its apo form and in complex with a p190RhoGAP phosphotyrosine peptide. PLOS ONE 2019, 14: e0226113. PMID: 31891593, PMCID: PMC6938330, DOI: 10.1371/journal.pone.0226113.Peer-Reviewed Original ResearchConceptsN-terminal SH2 domainSH2 domainPhosphotyrosine peptidesNative gel shiftSite-directed mutagenesisGAP proteinsCo-crystal structurePhosphorylated tyrosineRas pathwayUnliganded formApo formCross-talk occursGel shiftP120RasGAPIsothermal titration calorimetryP190RhoGAPCell growthSpecific conformationCell proliferationProteinX-ray crystal structureTitration calorimetryDisease pathogenesisCrystal structureRhoEvidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system
Hughes G, Hall S, Laxton C, Sridhar P, Mahadi A, Hatton C, Piggot T, Wotherspoon P, Leney A, Ward D, Jamshad M, Spana V, Cadby I, Harding C, Isom G, Bryant J, Parr R, Yakub Y, Jeeves M, Huber D, Henderson I, Clifton L, Lovering A, Knowles T. Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system. Nature Microbiology 2019, 4: 1692-1705. PMID: 31235958, DOI: 10.1038/s41564-019-0481-y.Peer-Reviewed Original ResearchConceptsMla pathwayInner membraneAsymmetric Gram-negative outer membranePhospholipid transportRetrograde phospholipid transportGram-negative outer membranePhospholipid-binding pocketABC transport systemSoluble periplasmic proteinBacterial inner membraneInner membrane ATPaseIndependent of ATPClosed apo conformationPhospholipid exportPeriplasmic proteinsMlaFEDB complexOuter membraneApo formApo conformationLipid exportMembrane ATPaseExport processPathwayMembraneMLAC
2008
Structural basis for base discrimination by RB69 DNA polymerase
Wang M, Klimenko D, Steitz T, Wang J. Structural basis for base discrimination by RB69 DNA polymerase. The FASEB Journal 2008, 22: 593.2-593.2. DOI: 10.1096/fasebj.22.1_supplement.593.2.Peer-Reviewed Original ResearchTriple mutantApo formStructural basisBase pairsDNA polymeraseReplicative DNA polymerasesWild-type enzymeTernary complexTemplating baseHelix PBase selectivityNascent base pairRB69 DNA polymeraseBase discriminationWild-type PolType enzymeMismatched base pairsMutantsPol mutantsRB69 polPolymeraseComplexesS565Y416Pol
2006
Solution Structure and Backbone Dynamics of an Endopeptidase HycI from scherichia coli IMPLICATIONS FOR MECHANISM OF THE [NiFe] HYDROGENASE MATURATION*
Yang F, Hu W, Xu H, Li C, Xia B, Jin C. Solution Structure and Backbone Dynamics of an Endopeptidase HycI from scherichia coli IMPLICATIONS FOR MECHANISM OF THE [NiFe] HYDROGENASE MATURATION*. Journal Of Biological Chemistry 2006, 282: 3856-3863. PMID: 17150961, DOI: 10.1074/jbc.m609263200.Peer-Reviewed Original ResearchConceptsSolution structureMetal ion titration experimentsApo formBackbone dynamics studiesMolecular mechanisms of recognitionDynamics studiesMetabolism of hydrogenC-terminal cleavageHydrogenase 3Substrate recognitionCrystal structureFamily proteinsMechanism of recognitionTitration experimentsEscherichia coliBackbone dynamicsCleavage processClosed conformationHycIBiological functionsBiological processesMolecular mechanismsEndopeptidaseM52Cleavage
2005
Crystal Structures of Proto-oncogene Kinase Pim1: A Target of Aberrant Somatic Hypermutations in Diffuse Large Cell Lymphoma
Kumar A, Mandiyan V, Suzuki Y, Zhang C, Rice J, Tsai J, Artis D, Ibrahim P, Bremer R. Crystal Structures of Proto-oncogene Kinase Pim1: A Target of Aberrant Somatic Hypermutations in Diffuse Large Cell Lymphoma. Journal Of Molecular Biology 2005, 348: 183-193. PMID: 15808862, DOI: 10.1016/j.jmb.2005.02.039.Peer-Reviewed Original ResearchMeSH KeywordsAdenylyl ImidodiphosphateAmino Acid SequenceApoproteinsCrystallography, X-RayHumansLymphoma, Large B-Cell, DiffuseModels, MolecularMolecular Sequence DataMutationProtein BindingProtein ConformationProtein Serine-Threonine KinasesProto-Oncogene MasProto-Oncogene ProteinsProto-Oncogene Proteins c-pim-1Sequence AlignmentConceptsKinase activitySerine/threonine kinaseAberrant somatic hypermutationSomatic hypermutationKinase inhibitor scaffoldN-terminal lobePim1 mutantsTypical kinasesCo-crystal structureThreonine kinaseProtein kinaseBackbone hydrogen bondsKinase PIM1Apo formBiological functionsProline residuesPIM1 inhibitorsNovel chemical classUnique structural featuresLow molecular massInhibitor scaffoldsCell survivalMolecular massPosition 123PIM1
2003
The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases
Kamtekar S, Kennedy WD, Wang J, Stathopoulos C, Söll D, Steitz TA. The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 1673-1678. PMID: 12578991, PMCID: PMC149891, DOI: 10.1073/pnas.0437911100.Peer-Reviewed Original ResearchConceptsLigand-free conformationCognate amino acidAmino acidsRecent biochemical experimentsProlyl-tRNA synthetasesCysteinyl-tRNA synthetaseProlyl-tRNA synthetaseActive site pocketMethanocaldococcus jannaschiiMethanopyrus kandleriMethanothermobacter thermautotrophicusCognate tRNAEssential enzymeApo formStructural basisBiochemical experimentsAminoacyl-adenylate analoguesHomology modelingConformational changesProtein synthesisTRNAProRSAdenylate complexNanomolar affinitySynthetase
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