Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F - Wikidata - thesis-toulmin - TriplyDB

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

http://www.wikidata.org/entity/Q27682423

about

Visualizing functional motions of membrane transporters with molecular dynamics simulations Post-expression strategies for structural investigations of membrane proteins.Thermodynamics of ABC transporters Structural basis for a homodimeric ATPase subunit of an ECF transporter Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state Imperfect coordination chemistry facilitates metal ion release in the Psa permease Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F Structure and mechanism of an active lipid-linked oligosaccharide flippase Towards structural systems pharmacology to study complex diseases and personalized medicine Systematic detection of internal symmetry in proteins using CE-Symm Effects of lipid environment on the conformational changes of an ABC importer.Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter.Structural basis of inhibition of lipid-linked oligosaccharide flippase PglK by a conformational nanobody.Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment.Conformational dynamics of the nucleotide binding domains and the power stroke of a heterodimeric ABC transporter.Structural diversity of ABC transporters.Advances in the molecular understanding of biological zinc transport.Apo, Zn2+-bound and Mn2+-bound structures reveal ligand-binding properties of SitA from the pathogen Staphylococcus pseudintermedius.Structure of a pantothenate transporter and implications for ECF module sharing and energy coupling of group II ECF transporters.In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.The allosteric regulatory mechanism of the Escherichia coli MetNI methionine ATP binding cassette (ABC) transporter ATP-Binding Cassette Transporter Structure Changes Detected by Intramolecular Fluorescence Energy Transfer for High-Throughput Screening.Conformational Motions and Functionally Key Residues for Vitamin B12 Transporter BtuCD-BtuF Revealed by Elastic Network Model with a Function-Related Internal Coordinate ATP Hydrolysis Induced Conformational Changes in the Vitamin B12 Transporter BtuCD Revealed by MD Simulations.The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism A vitamin B₁₂ transporter in Mycobacterium tuberculosis.A single intact ATPase site of the ABC transporter BtuCD drives 5% transport activity yet supports full in vivo vitamin B12 utilization.EPR spectroscopy of MolB2C2-a reveals mechanism of transport for a bacterial type II molybdate importer Manganese acquisition and homeostasis at the host-pathogen interface.Conformational Change of a Tryptophan Residue in BtuF Facilitates Binding and Transport of Cobinamide by the Vitamin B12 Transporter BtuCD-F.Sustainable growth of Dehalococcoides mccartyi 195 by corrinoid salvaging and remodeling in defined lactate-fermenting consortia Molecular mechanism of the Escherichia coli maltose transporter.Vitamin B(12) metabolism in Mycobacterium tuberculosis.Diversity in ABC transporters: type I, II and III importers.The uncoupled ATPase activity of the ABC transporter BtuC2D2 leads to a hysteretic conformational change, conformational memory, and improved activity.Invited review: Architectures and mechanisms of ATP binding cassette proteins.Biophysical Approaches Facilitate Computational Drug Discovery for ATP-Binding Cassette Proteins.Mechanistic diversity in ATP-binding cassette (ABC) transporters.Structural and mechanistic diversity of multidrug transporters.

P2860

Q26826746-662B3527-962A-421C-AB99-FC9130F252F8 Q26849743-B8AF3CF1-51A4-4BCE-B3CA-E1957C2FF1F8 Q27340177-FE5458FE-47A6-471C-A18C-0E119729EA4F Q27680198-328A14FC-967A-424F-B6C2-5C3991FE892A Q27684301-930F46E5-D385-41EC-BAC1-8EB6C8706F0D Q27687486-E48E2F6E-D729-4795-A6A8-73DC19F139E6 Q27696181-55A4DB20-739F-49B7-B8CF-14CF33394FDE Q27701786-AC18C5ED-0E32-45B1-B15C-0F384AB302BE Q28538838-9F700843-6163-40A6-A7EE-84FA3687BCB5 Q28645866-8C52F6CF-3821-4500-AC1C-2C57E371BE03 Q30362800-6E849312-8A78-4F2C-9FAB-E4F001EB5D37 Q30601389-EABD78B1-76C5-4A55-921E-670CA51E8DE2 Q33577108-502DC700-2A31-4195-A76D-7790BB779CF7 Q33652199-25609ECF-EE9B-4933-83D9-E6155D36F14A Q33715209-BE8615AF-7DAA-4981-B079-06251C8FDFC5 Q34410603-A634E4C1-06A9-4991-AA49-DE2131A4A68C Q34459994-C42CA315-8503-4886-A161-2893FD794599 Q34564114-294500DE-D616-45A2-8F48-CE6F5979E597 Q34830411-DAFA01FD-1DA8-4CFE-B1C1-F52DB0D166CB Q35126649-4EBBEE85-505A-42A0-AD5C-A27CE6AB5A7D Q35580861-14446109-D0B2-4B9A-A721-ED1D55AF4D18 Q35617947-12F06FB7-5991-4CA5-90D5-3F27E14CE055 Q36088524-96BE3ED3-E52A-4841-99F2-5F47CE9AADDA Q36199911-BEFA258A-C9F6-4CCA-9B57-4FD7DEA562C7 Q36208567-05F7E6F1-8D6F-41C7-BD0B-9AB3B1EF1D9A Q36253391-18B3B2FA-3AA2-42DA-95AB-BF057A20F17D Q36702412-BFB0DDCE-59CA-4853-9ADE-03567F02C2AD Q36747821-A7476E6B-5C29-4529-9D9F-0DCA1C906281 Q37175170-BB0CF252-E6E6-49F8-88E4-F6C3B12CACA4 Q37365396-CEE1C6F6-61B3-46E7-9C39-B971508F3A62 Q37609518-5062B1C2-0E57-46A2-857B-0B61C1437FCE Q37712883-6B97C6B5-DCF0-4A39-B626-47EDE814CD4B Q38102823-6C7F7B3C-0F64-44E2-8749-F9365E976340 Q38160534-5BB40B40-5D38-42AA-BFF9-8FAB961D096D Q38243039-FC67C650-2F2D-4400-AD1E-897923E738A1 Q38612234-724954AD-B1F5-457B-A3A1-0419FEC0A6CB Q38796195-C0844274-EE94-4C75-AB4F-2C613F703FF8 Q38837398-0995C569-216A-42F3-BEC5-041C45401B07 Q38856661-33773C00-8DAC-41EF-AFFD-992B75345FC6 Q38912551-D6B7461A-0DB4-48A4-A9EB-32BD0167F08C

P2860

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

http://www.wikidata.org/entity/Q27682423

description

2012 nî lūn-bûn

@nan

2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@ast

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@en

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@nl

type

label

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@ast

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@en

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@nl

prefLabel

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@ast

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@en

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@nl

P1433

Q27682423-9F3EE67D-8A27-4193-B2F1-FBC483A6FB34

P1476

Q27682423-C3008E20-AA1F-479A-9460-B2F78C2B9EC8

P2093

Q27682423-23D408A7-1505-49EA-80BB-BDDC08EC91BF

Q27682423-309A01E2-FC86-4C03-A2E0-B35E9BB0951B

Q27682423-43CC7724-CE12-4F5A-A5E1-37F68736613A

P2860

Q27682423-061E630C-BFE9-4A38-BF21-748936F13323

Q27682423-0790935A-F26B-4EDC-BD5A-993BF1749440

Q27682423-0C07DA0E-C1CA-4374-B282-CF88660C8277

Q27682423-0C63B321-66D5-4E12-8188-EEE3A2673998

Q27682423-0D5B1488-CD59-44C3-981E-23F4A120EF33

Q27682423-0D8ED3D8-423F-4ED9-8F3B-310F14CA1A2B

Q27682423-10B7BF32-FE60-4738-80AD-E46E17C9807A

Q27682423-1529E473-EDCE-48DC-85B8-20614103F083

Q27682423-17E4C28C-F604-4521-A9A3-3A6882AFAF58

Q27682423-27E170E2-03B2-45BE-82D9-EBCDF9829965

P2888

Q27682423-48AEB20B-AF1E-448B-B664-33AAA8E90553

P304

Q27682423-7ED3338D-8240-427F-A537-E1A2BA81DE36

P31

Q27682423-B98A931C-0B66-4951-8D2B-247F54D05172

P356

Q27682423-F74B4E77-D6AB-4823-977F-A01F49EFBF9A

P407

Q27682423-CE50BC5E-3538-426E-924A-EB11C9F10A81

P433

Q27682423-1285B608-3CE7-49EE-9900-357736359E82

P478

Q27682423-AC3D1BC1-2C5F-4556-8CA6-7D4C2A5A7BED

P577

Q27682423-2C5FFC4A-E059-4F16-A5DF-7F5BA5011F35

P6179

Q27682423-4D6CD431-889C-4509-81E8-8C3895AE1F80

P698

Q27682423-872995C4-0750-446E-BD9B-6725CA948BBA

P921

Q27682423-052DDB66-4231-40CA-A27A-31314F2D1C66

Q27682423-6feb3957-5c61-413b-83b5-bf3b0f977ffe

Q27682423-b8fb7578-4587-426c-9169-41d25f15df5e

P356

P1433

P1476

Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F

@en

P2093

Kaspar P Locher

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

Samantha A Mireku

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

Vladimir M Korkhov

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

P2860

H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

ABC transporters: the power to change

Structure, function, and evolution of bacterial ATP-binding cassette systems

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Flexibility in the ABC transporter MsbA: Alternating access with a twist.

Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily

The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism

Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding

The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter

P2888

P304

367-72

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

P31

scholarly article

P356

10.1038/NATURE11442

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

P407

P433

7420

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

P478

490

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

P577

2012-10-18T00:00:00Z

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

P6179

1023983550

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

P698

23000901

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

P921