The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded.

scientific article published on 7 August 2015

The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded. is …
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scholarly articleQ13442814

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P356DOI10.1016/J.JMB.2015.07.024
P932PMC publication ID4579052
P698PubMed publication ID26259880

P50authorClarice de Azevedo SouzaQ85887347
P2093author name stringRoberto N De Guzman
Gregory V Plano
Sukanya Chaudhury
P2860cites workCLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceQ24286950
LcrG-LcrV interaction is required for control of Yops secretion in Yersinia pestisQ24548891
Roles of LcrG and LcrV during type III targeting of effector Yops by Yersinia enterocoliticaQ24548902
Interaction of the Yersinia pestis type III regulatory proteins LcrG and LcrV occurs at a hydrophobic interfaceQ24797087
Assembly and structure of the T3SSQ26865556
Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cellsQ27028058
The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plagueQ27643133
NMR Structure of the N-terminal Coiled Coil Domain of the Andes Hantavirus Nucleocapsid ProteinQ27651453
Structural Instability Tuning as a Regulatory Mechanism in Protein-Protein InteractionsQ27676032
Substrate-Activated Conformational Switch on Chaperones Encodes a Targeting Signal in Type III SecretionQ27676993
Structure of theYersinia pestistip protein LcrV refined to 1.65 Å resolutionQ27678232
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxationQ27860508
Using NMRView to visualize and analyze the NMR spectra of macromoleculesQ27860567
NMRPipe: a multidimensional spectral processing system based on UNIX pipesQ27860859
The PSIPRED protein structure prediction serverQ27860953
The type III secretion injectisomeQ29617944
Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy.Q30360846
Virulence role of V antigen of Yersinia pestis at the bacterial surfaceQ30778457
EspB from enterohaemorrhagic Escherichia coli is a natively partially folded proteinQ30981321
Yersinia type III secretion: send in the effectorsQ34774578
The Yersinia Ysc-Yop 'type III' weaponryQ34931776
Control of effector export by the Pseudomonas aeruginosa type III secretion proteins PcrG and PcrV.Q35071514
Yersinia pestis LcrV forms a stable complex with LcrG and may have a secretion-related regulatory role in the low-Ca2+ responseQ35620091
LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestisQ36101650
The Salmonella type III secretion system inner rod protein PrgJ is partially folded.Q36127196
Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMRQ36280194
Positional preference of proline in alpha-helicesQ36281580
What's the point of the type III secretion system needle?Q36638746
Roles of YopN, LcrG and LcrV in controlling Yops secretion by Yersinia pestis.Q36984033
Structure and biophysics of type III secretion in bacteriaQ37014297
Effectors of animal and plant pathogens use a common domain to bind host phosphoinositidesQ37167670
Linking folding and bindingQ37373866
Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studiesQ37592032
Intrinsically disordered proteins: regulation and diseaseQ37868137
LcrG is required for efficient translocation of Yersinia Yop effector proteins into eukaryotic cells.Q39571764
DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of Yersinia pestis KIM5.Q39573090
The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE.Q40642883
Regulation by Ca2+ in the Yersinia low-Ca2+ responseQ40840513
Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU proteinQ41381050
The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needlesQ41456399
Interactions of the type III secretion pathway proteins LcrV and LcrG from Yersinia pestis are mediated by coiled-coil domains.Q41471377
PcrG protects the two long helical oligomerization domains of PcrV, by an interaction mediated by the intramolecular coiled-coil region of PcrG.Q41895565
NMR characterization of the interaction of the Salmonella type III secretion system protein SipD and bile saltsQ42126458
Inter-molecular coiled-coil formation in human apolipoprotein E C-terminal domainQ44659103
An optimized system for expression and purification of secreted bacterial proteinsQ45076251
Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurementsQ46172640
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein foldingQ46559043
Amphipathic alpha-helix bundle organization of lipid-free chicken apolipoprotein A-I.Q50519411
Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coilsQ70648566
Coiled-coil domains in proteins secreted by type III secretion systemsQ73663925
Protein chemical shift analysis: a practical guideQ77922368
P433issue19
P407language of work or nameEnglishQ1860
P921main subjectYersinia pestisQ153875
molecular chaperonesQ422496
protein foldingQ847556
P304page(s)3096-3109
P577publication date2015-08-07
P1433published inJournal of Molecular BiologyQ925779
P1476titleThe LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded
P478volume427

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Q64075941The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cellscites workP2860

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