Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
about
The Membrane Steps of Bacterial Cell Wall Synthesis as Antibiotic TargetsMuraymycin nucleoside-peptide antibiotics: uridine-derived natural products as lead structures for the development of novel antibacterial agentsStructural Insights into Protein-Protein Interactions Involved in Bacterial Cell Wall BiogenesisResistance to antibiotics targeted to the bacterial cell wallCore Steps of Membrane-Bound Peptidoglycan Biosynthesis: Recent Advances, Insight and OpportunitiesCrystal structure of lipid phosphatase Escherichia coli phosphatidylglycerophosphate phosphatase BStructure and mechanism of an intramembrane liponucleotide synthetase central for phospholipid biosynthesisAnalyzing native membrane protein assembly in nanodiscs by combined non-covalent mass spectrometry and synthetic biologyStructural insights into inhibition of lipid I production in bacterial cell wall synthesis.Structural basis for catalysis at the membrane-water interface.Analysis of MreB interactors in Chlamydia reveals a RodZ homolog but fails to detect an interaction with MraYAmino acid motifs in natural products: synthesis of O-acylated derivatives of (2S,3S)-3-hydroxyleucine.Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli.Analysis of a dual domain phosphoglycosyl transferase reveals a ping-pong mechanism with a covalent enzyme intermediate.Chemoenzymatic syntheses of water-soluble lipid I fluorescent probes.New Structural Templates for Clinically Validated and Novel Targets in Antimicrobial Drug Research and Development.Total Synthesis of Dansylated Park's Nucleotide for High-Throughput MraY Assays.Lipid Requirements for the Enzymatic Activity of MraY Translocases and in Vitro Reconstitution of the Lipid II Synthesis PathwayImproving the N-terminal diversity of sansanmycin through mutasynthesis.Structure-function relationships of membrane-associated GT-B glycosyltransferases.The giant protein Ebh is a determinant of Staphylococcus aureus cell size and complement resistance.A Modular Approach to Phosphoglycosyltransferase Inhibitors Inspired by Nucleoside Antibiotics.New Insight into the Catalytic Mechanism of Bacterial MraY from Enzyme Kinetics and Docking Studies.N-Acetylglucosamine-1-phosphate transferase, WecA, as a validated drug target in Mycobacterium tuberculosis.Bacteriological profiling of diphenylureas as a novel class of antibiotics against methicillin-resistant Staphylococcus aureus.A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer.Targeting the gram-negative bacteria peptidoglycan synthase MraY as a new approach for monoclonal antibody anti-bacterial activity.Membrane Interaction of the Glycosyltransferase WaaG.TarO-specific inhibitors of wall teichoic acid biosynthesis restore β-lactam efficacy against methicillin-resistant staphylococci.Conservation and Covariance in Small Bacterial Phosphoglycosyltransferases Identify the Functional Catalytic CoreA Rapid and Efficient Luminescence-based Method for Assaying Phosphoglycosyltransferase Enzymes.Ligand Shaping in Induced Fit Docking of MraY Inhibitors. Polynomial Discriminant and Laplacian Operator as Biological Activity Descriptors.Structural Investigation of Park's Nucleotide on Bacterial Translocase MraY: Discovery of Unexpected MraY Inhibitors.Mechanism of action of the uridyl peptide antibiotics: an unexpected link to a protein-protein interaction site in translocase MraY.Identification of a novel inhibition site in translocase MraY based upon the site of interaction with lysis protein E from bacteriophage ϕX174.Lipid II overproduction allows direct assay of transpeptidase inhibition by β-lactams.Quinovosamycins: new tunicamycin-type antibiotics in which the α, β-1″,11'-linked N-acetylglucosamine residue is replaced by N-acetylquinovosamine.Selective catalytic hydrogenation of the N-acyl and uridyl double bonds in the tunicamycin family of protein N-glycosylation inhibitors.Modified tunicamycins with reduced eukaryotic toxicity that enhance the antibacterial activity of β-lactams.Bacterial phosphoglycosyl transferases: initiators of glycan biosynthesis at the membrane interface.
P2860
Q26738402-AA0C1A9E-4F3F-408A-A901-84B62600EC79Q26747275-070FDBB3-6EE8-4FC5-B3C2-17E8E5667AE7Q26748117-2F324B91-23E1-4108-9A70-B2A78353955DQ26859841-761EA450-6129-4B23-A61E-D7C24D49229BQ27025371-A5A9F4D6-2439-4123-B2BE-B733A62FBE74Q27683761-E3E50705-DEFA-47B3-ACBF-220B00125CEAQ27684474-FAD854A7-1A73-4FC9-B6E5-33F9E4C5AB86Q28817540-15AC8397-9C88-4864-8815-916FD4634D34Q28833309-9A55D7FF-339C-48D4-93FC-0B5A4D5DA22CQ30152692-EA6F5674-015A-405B-8ECC-BF801AC59734Q33719244-66D367F3-49BC-4C30-B559-E057C31B0F7AQ33829573-D803A6B5-E134-46D3-9E54-437D3A332E88Q33846415-10966A7B-CE19-4DDD-8EBA-ADFB58705908Q33887056-F633723A-0558-4D77-82D5-9FA7DD0B3BC0Q35860419-C5B00BD9-2E25-4131-AD65-A261A611C585Q36153263-6B08920F-DF74-484F-9946-934FD8CC428FQ36176949-21551FAA-EDA2-4D94-A4BC-FA8629E15892Q36518393-D6FB88A2-5E71-453D-B31C-A50E1C283B7FQ36876039-2C97B45F-5245-47E8-8142-08422CDED51DQ37532999-B177A445-8B89-4FF9-87A9-38D0A45E60FFQ37643393-8726309C-09E6-4AE9-A537-1760F32062F9Q38932509-5D0FAC13-702E-4090-95F5-5D51B760D22BQ39735310-2D2DF2C6-0144-4DD3-934F-888ECD0A402CQ40065984-AD125D5B-460A-4C0C-9FC5-41A397BBDB11Q40098505-16B53D57-F3B5-4872-AB77-E8F463299A87Q40132165-88805D93-F8FC-496A-BD5A-59020E6A6F70Q40176262-C053EF4B-C524-4902-A690-E11A4E81A3E1Q40658189-89B580BF-1F4C-4FCD-AE36-A01ED8CD93E3Q40760998-36B18391-004E-4E4D-97EE-EB1EE197A2A5Q41050878-7DF5BE3F-8BE1-4E28-8210-BE032DC47735Q41084514-8096A92A-4287-4CFA-9EFE-5784FE8E3A81Q41181539-F8CD9EC4-5592-4763-A543-59037017450CQ41729149-01C64C58-E5CC-4538-A559-96F4A2240890Q42187998-F41CFB72-6653-44EA-B75E-FA8D54A13E64Q42214738-C4CE9D60-4CA7-446F-A27C-9BFFD19C858CQ44699614-32130A98-371F-4632-A409-73AB975F4E3EQ46400754-67421429-5646-425F-B59B-0E5A9F678B87Q47580500-D6E76D26-8440-4552-8754-C9369C7B3EA2Q47738775-950067F8-9D15-44C6-9C12-5A7D86621867Q47949690-30A383D7-537C-487A-8539-456DC51CAAA5
P2860
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
description
2013 nî lūn-bûn
@nan
2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@ast
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@en
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@nl
type
label
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@ast
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@en
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@nl
prefLabel
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@ast
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@en
Crystal Structure of MraY, an Essential Membrane Enzyme for Bacterial Cell Wall Synthesis
@nl
P2093
P2860
P3181
P356
P1433
P1476
Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis
@en
P2093
Ben C Chung
Do-Yeon Kwon
Jinshi Zhao
Jiyong Hong
Robert A Gillespie
Seok-Yong Lee
Ziqiang Guan
P2860
P304
P3181
P356
10.1126/SCIENCE.1236501
P407
P50
P577
2013-08-01T00:00:00Z