Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits - Wikidata - wikimedia - TriplyDB

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

http://www.wikidata.org/entity/Q27641045

about

sameAs

Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout Lessons in Fundamental Mechanisms and Diverse Adaptations from the 2015 Bacterial Locomotion and Signal Transduction Meeting Structural Features Reminiscent of ATP-Driven Protein Translocases Are Essential for the Function of a Type III Secretion-Associated ATPase.Crystal structure of the C-terminal domain of the Salmonella type III secretion system export apparatus protein InvA Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases Architecture of the major component of the type III secretion system export apparatus Substrate-Activated Conformational Switch on Chaperones Encodes a Targeting Signal in Type III Secretion Type Three Secretion System in Attaching and Effacing Pathogens Interaction of the extreme N-terminal region of FliH with FlhA is required for efficient bacterial flagellar protein export Common evolutionary origin for the rotor domain of rotary ATPases and flagellar protein export apparatus EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Deciphering the assembly of the Yersinia type III secretion injectisome.Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus.Interactions between flagellar and type III secretion proteins in Chlamydia pneumoniae.Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA Identification of the docking site between a type III secretion system ATPase and a chaperone for effector cargo.Bacterial nanomachines: the flagellum and type III injectisome.Molecular architecture of the bacterial flagellar motor in cells The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis.Structural diversity of bacterial flagellar motors.An energy transduction mechanism used in bacterial flagellar type III protein export.ATPase-independent type-III protein secretion in Salmonella enterica.Mutations in the Borrelia burgdorferi Flagellar Type III Secretion System Genes fliH and fliI Profoundly Affect Spirochete Flagellar Assembly, Morphology, Motility, Structure, and Cell Division.Molecular Models for the Core Components of the Flagellar Type-III Secretion Complex.Cytoskeletal "jellyfish" structure of Mycoplasma mobile.Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator.FliH and FliI ensure efficient energy coupling of flagellar type III protein export in Salmonella.Flagellar biogenesis of Xanthomonas campestris requires the alternative sigma factors RpoN2 and FliA and is temporally regulated by FlhA, FlhB, and FlgM.Recognition and targeting mechanisms by chaperones in flagellum assembly and operation High-Resolution pH Imaging of Living Bacterial Cells To Detect Local pH Differences.Membrane targeting and pore formation by the type III secretion system translocon.Building a secreting nanomachine: a structural overview of the T3SS.Building a flagellum outside the bacterial cell.From molecular evolution to biobricks and synthetic modules: a lesson by the bacterial flagellum.Type III secretion systems: the bacterial flagellum and the injectisome.Strategies to Block Bacterial Pathogenesis by Interference with Motility and Chemotaxis.Impact of the N-terminal secretor domain on YopD translocator function in Yersinia pseudotuberculosis type III secretion.Assembly and stoichiometry of the core structure of the bacterial flagellar type III export gate complex.Mechanism of type-III protein secretion: Regulation of FlhA conformation by a functionally critical charged-residue cluster.

P2860

Q24644829-C11A4F49-144A-4565-96AA-029A4C58260C Q26801520-42C7F8E4-8070-42F0-AE49-4FEDC1FB59B1 Q27322401-BF3F3AE0-41D4-45DF-99E2-C135C845A9E1 Q27660301-A8607318-CEB8-4A74-A845-20BE20A1F480 Q27666617-90D5AEEC-E477-451F-9970-578B0B4050C1 Q27675415-4F6D8C99-AA6B-4859-9BC9-08B2E7E01E7C Q27676993-56B91E6D-F7C5-4181-B6F9-9A623A33E628 Q28074332-C4DD6ECB-4467-4EB4-94FB-F62D5D17A871 Q28490035-C130CD7C-A78C-4C19-9BA7-6E2D294A3B69 Q28533330-054189C3-813B-4A42-A7D5-64F7912C2DB0 Q28536457-9902E3AA-FE05-4524-ABEA-6E0EE49BFC9D Q30318075-5E353E29-8A60-4151-BB83-CA4C3D2CAD91 Q30494891-BE207E25-9AD6-4127-B152-ED4A695C9227 Q30588899-22C15BAF-4804-469D-82F4-0594CA7BC4B6 Q33526048-3F28DB2F-6834-444E-A411-AE7B73BD7FDC Q33979924-3478BA67-AB0A-4413-B629-3919CAC7A35B Q34141168-068575B1-EAD3-4261-9405-2FEE4E53439C Q34142106-08C0AA20-8FE5-4E9B-A243-CEF9EFE15265 Q34459768-90FB343B-689A-46FD-A041-64F9DCBBC491 Q34755400-F23D8557-3C40-424F-BD17-E84DE9FA5552 Q35177207-9082F251-D9B7-4357-ADF1-BF4CA54D8E3B Q35367067-248D28A5-C031-4F8D-BF10-374A9B47226B Q35416990-3A52E582-8868-4E96-8369-327083707C16 Q35620167-770E3ACC-67EA-4720-A53F-807302669AD9 Q36195044-18537C1C-6B14-4CF3-AA24-96AE53D8FE8E Q36288692-0716522B-8463-40AE-B097-666775292D44 Q36770466-7639B512-D969-4792-8747-3DF899BD1666 Q36999741-D9B3FB46-F8CD-4748-9653-C0814C796260 Q37127844-AAB267E0-BE67-44D3-B434-CF117456C6AE Q37258436-F522F682-ADA8-4862-96E1-112C4D174CF7 Q37481747-35BD0914-34D2-4539-BC33-55207DA98DAE Q37823656-E5E55752-38A7-40AB-9319-FBB15DD41CBA Q38202459-D396F8CF-46E0-4E34-96C8-AB06CC3C81E7 Q38224001-951FD7E6-C09F-4A76-BE5D-D71648B28D51 Q38229427-F12CC6ED-5032-4132-8737-1EC68DF80E21 Q38586932-4ECDFD9C-8CDC-48A2-ADA2-68590A6D1BA3 Q38783540-A866DA23-9254-4E6A-BC34-0E3D6369A5C7 Q39464419-E0E6C93C-E3FF-45B0-B6AB-EE22C8439BD9 Q40108405-4BB01CE3-11A0-48EB-B90D-22CBC329A70B Q40364421-C8191321-8622-4112-B004-625341E7B924

P2860

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

http://www.wikidata.org/entity/Q27641045

description

2007 nî lūn-bûn

@nan

2007 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@ast

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@en

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@nl

type

label

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@ast

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@en

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@nl

prefLabel

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@ast

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@en

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@nl

P1433

Q27641045-9914C586-5900-4408-93E9-A4CEA226F9E6

P1476

Q27641045-64D8C227-BB6A-430D-A781-055FB55258EE

P2093

Q27641045-2F12B66E-6F9A-4665-81DF-A32D74775AA6

Q27641045-8268E562-5523-45DD-A993-428F065454A9

Q27641045-D20CEE47-ECDA-46B0-B367-BD52A7108349

P2860

Q27641045-01831E4D-9D6C-4307-B314-F38CCFEB9933

Q27641045-024FE603-062D-4633-8FB9-4E099D889877

Q27641045-05D36D19-85A0-464F-845D-7F7EEB97A364

Q27641045-064749CE-8060-4223-927B-4E23BF6D3026

Q27641045-0FC834CF-7F25-4477-8A41-099A8B4188BB

Q27641045-1361749E-12A4-41B3-A2F7-8C05C50B9781

Q27641045-21EA6570-5769-49D1-8B04-9CB109D5432C

Q27641045-2E9ED369-4C66-4D03-AE35-0C0255212BD6

Q27641045-30B71321-B4C3-4B15-A42B-23F54D7CD49F

Q27641045-348AD38B-696C-4DDD-B3C1-9E742D72E843

P304

Q27641045-FAF8EAED-A165-4428-A36E-98E6D8D29941

P31

Q27641045-6CB996BD-0B80-4CBD-8CDC-C7A1DD76EF9E

P3181

Q27641045-AF0371FE-3261-4EEB-98DF-D56FC55EAAAC

P356

Q27641045-CD4A3F8A-F38C-46DB-AF21-521C26796002

P407

Q27641045-73B73BE5-917F-462D-8C7A-CB957649C899

P433

Q27641045-D497F34E-A248-4591-909D-FFAE57304835

P478

Q27641045-E0BA2910-D2B4-4DDB-88B2-AF36A663BC38

P50

Q27641045-3F6FD9E1-D950-4A59-B55F-21569B2FFF26

P577

Q27641045-BA72AF0B-DBB4-4E4C-A200-3C3504242D8C

P5875

Q27641045-E018217F-4BD4-4C9E-834B-D7E8F4CD946C

P698

Q27641045-EB1FA5FB-7FC5-43B0-8315-749EA9287284

P932

Q27641045-290C2C98-D2DD-4B10-96D9-DD28D3001D28

P3181

P356

PNAS.0608090104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits

@en

P2093

Aiko Tahara

http://www.w3.org/2001/XMLSchema#string

Katsumi Imada

http://www.w3.org/2001/XMLSchema#string

Tohru Minamino

http://www.w3.org/2001/XMLSchema#string

P2860

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The structures of HsIU and the ATP-dependent protease HsIU-HsIV

Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer

Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein

P304

485-90

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2850362

http://www.w3.org/2001/XMLSchema#string

P356

10.1073/PNAS.0608090104

http://www.w3.org/2001/XMLSchema#string

P407

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

104

http://www.w3.org/2001/XMLSchema#string

P50

P577

2007-01-09T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

6599237

http://www.w3.org/2001/XMLSchema#string

P698

17202259

http://www.w3.org/2001/XMLSchema#string

P932

1766411

http://www.w3.org/2001/XMLSchema#string