Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features
about
Initiation of mRNA translation in bacteria: structural and dynamic aspectsThe 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analoguetRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates bindingThe crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetaseMechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase.A conserved structural motif at the N terminus of bacterial translation initiation factor IF2The 1.6 Å Crystal Structure of Mycobacterium smegmatis MshC: The Penultimate Enzyme in the Mycothiol Biosynthetic Pathway †Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP)Switching from an Induced-Fit to a Lock-and-Key Mechanism in an Aminoacyl-tRNA Synthetase with Modified SpecificityInsights into Function, Catalytic Mechanism, and Fold Evolution of Selenoprotein Methionine Sulfoxide Reductase B1 through Structural AnalysisStructure of Leishmania major methionyl-tRNA synthetase in complex with intermediate products methionyladenylate and pyrophosphateDistinct States of Methionyl-tRNA Synthetase Indicate Inhibitor Binding by Conformational SelectionStructures of Trypanosoma brucei methionyl-tRNA synthetase with urea-based inhibitors provide guidance for drug design against sleeping sicknessBrucella melitensis Methionyl-tRNA-Synthetase (MetRS), a Potential Drug Target for BrucellosisSelectivity and specificity of substrate binding in methionyl-tRNA synthetase.Two distinct domains of the beta subunit of Aquifex aeolicus leucyl-tRNA synthetase are involved in tRNA binding as revealed by a three-hybrid selection.Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acidsInitiation of protein synthesis in bacteria.Comparison of histidine recognition in human and trypanosomatid histidyl-tRNA synthetases.A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylationMisacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase.Rare recessive loss-of-function methionyl-tRNA synthetase mutations presenting as a multi-organ phenotype.Structural basis for amino acid and tRNA recognition by class I aminoacyl-tRNA synthetases.Structural and biochemical analysis of mammalian methionine sulfoxide reductase B2A study of communication pathways in methionyl- tRNA synthetase by molecular dynamics simulations and structure network analysisBiallelic Mutations of Methionyl-tRNA Synthetase Cause a Specific Type of Pulmonary Alveolar Proteinosis Prevalent on Réunion Island.Identification and Characterization of a Chemical Compound that Inhibits Methionyl-tRNA Synthetase from Pseudomonas aeruginosa.Evidence for late resolution of the aux codon box in evolution.Primary Structure Revision and Active Site Mapping of E. Coli Isoleucyl-tRNA Synthetase by Means of Maldi Mass SpectrometryDiscovery of Escherichia coli methionyl-tRNA synthetase mutants for efficient labeling of proteins with azidonorleucine in vivoToward the catalytic mechanism of a cysteine ligase (MshC) from Mycobacterium smegmatis: an enzyme involved in the biosynthetic pathway of mycothiol.Emergence and evolution.let-65 is cytoplasmic methionyl tRNA synthetase in C. elegans.Probing the global and local dynamics of aminoacyl-tRNA synthetases using all-atom and coarse-grained simulations.Crystallization of Mycobacterium smegmatis methionyl-tRNA synthetase in the presence of methionine and adenosine.Toward an era of utilizing methionine overproducing hosts for recombinant protein production in Escherichia coli.Global tRNA misacylation induced by anaerobiosis and antibiotic exposure broadly increases stress resistance in Escherichia coli.Mode of action and biochemical characterization of REP8839, a novel inhibitor of methionyl-tRNA synthetase.Inhibition of methionyl-tRNA synthetase by REP8839 and effects of resistance mutations on enzyme activity.
P2860
Q26799769-9EA2B771-6523-4EE5-8725-B33197724E3DQ27622535-6013C5D3-94DE-421E-A0C2-7A10BB9C67AEQ27627790-063101EA-0310-4887-BBB9-AD3A8F6F8B9CQ27629266-8F9E4981-5624-4C3E-8F90-623A41D04C17Q27639036-EFA273F9-DD35-4038-9D67-C46AFA43B3DCQ27640379-672A8ED8-1BA6-41F1-A8C2-1CED88C39C74Q27640582-1A4249E2-EA3B-4BDD-95BF-1C8B689BAFAFQ27653039-C7A69C7B-5D24-484F-A50F-7FA25228CBA3Q27656901-AF5DDD88-11CA-46E7-818F-26C9F36CB250Q27657833-89F495A3-9FF3-4887-A072-7F17EBFCFFA1Q27663173-770CF88C-CC59-42E1-A64B-D004CD472A74Q27666287-BF077195-3376-4877-B065-0F7217E3679FQ27671580-4A3226BE-5071-424F-A748-4BB3F24A52F6Q27683462-B1944D26-27B4-4A53-97A8-4B51358FF5D6Q28553414-14FDEA7A-723E-480A-A5CC-779C9DB6C9C9Q30343058-A0B5877B-01A8-432C-8A43-42575491E525Q33203997-5B1C7EF4-0088-4176-8FEA-D1DD3D8416B9Q33248009-1F8543A2-F556-4A02-A986-EEE6785DAE62Q34401329-9947CD2E-E17C-4835-8BBD-E438C3733AFAQ34603136-FE708940-E858-44F9-977B-989D611F4288Q34683911-460D1BBE-CDF8-4F0D-9307-F062DB525FECQ34880775-72573112-CD4F-4199-B1D8-BD9598AD8E1DQ35011198-E27AF0B1-AF3C-46EA-B8FD-8AE1DC024945Q35133650-A02D752C-5DB1-49B7-84EA-9F3FA06BF027Q35344420-0087DEC2-A54B-4A31-B3B8-5BC718674423Q36023760-DB8F9CA4-75E3-45D3-9F7E-3D14E8F5774DQ36060847-93561290-95FE-47F9-9DE0-4F9DA05C85E1Q36328636-B2B7CEA9-B7D7-47B5-BE64-F7E0B8B4A6B4Q37000566-B8947F56-CF84-4B2D-9B9A-EFAE818681ABQ37225462-A85E55DC-3F04-4DFA-A871-66DA730225DCQ37340804-69C427F0-B1DF-4FD6-B993-B322355E7C1AQ37356885-AF4D8F81-1E9B-4E2A-86A5-74DD38F28E89Q38088164-F987B820-706B-46DF-9C47-B996B01ED812Q38445788-641974FE-1E33-4806-A2EE-B7DFCCAF6863Q39851076-7F5E757A-5D52-4942-8FBC-340DF9485150Q41855356-C9911F71-482F-4586-9DBC-4C2940484EB7Q41957491-D909657A-E82D-41BF-87B6-8A0D6DAE8714Q42017335-F81CA65B-FB9C-4935-9C40-66191C4B90A8Q42565043-A2699061-0ECF-44CB-9781-52C8C90510DDQ43215569-8C055D7E-4757-49AD-A4F3-72320C4C968D
P2860
Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Crystal structure of Escherich ...... ghts species-specific features
@ast
Crystal structure of Escherich ...... ghts species-specific features
@en
Crystal structure of Escherich ...... ghts species-specific features
@nl
type
label
Crystal structure of Escherich ...... ghts species-specific features
@ast
Crystal structure of Escherich ...... ghts species-specific features
@en
Crystal structure of Escherich ...... ghts species-specific features
@nl
prefLabel
Crystal structure of Escherich ...... ghts species-specific features
@ast
Crystal structure of Escherich ...... ghts species-specific features
@en
Crystal structure of Escherich ...... ghts species-specific features
@nl
P2093
P50
P3181
P356
P1476
Crystal structure of Escherich ...... ghts species-specific features
@en
P2093
P304
P3181
P356
10.1006/JMBI.1999.3339
P407
P577
1999-12-17T00:00:00Z