Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system
about
Probing the dynamic distribution of bound states for methylcytosine-binding domains on DNASolution NMR Structures of Productive and Non-productive Complexes between the A and B Domains of the Cytoplasmic Subunit of the Mannose Transporter of the Escherichia coli Phosphotransferase SystemX-ray structures of the three Lactococcus lactis dihydroxyacetone kinase subunits and of a transient intersubunit complexSolution Structure of the IIAChitobiose-IIBChitobiose Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase SystemStructure of the Plasmodium 6-cysteine s48/45 domainSolution Structure of a Complex of the Histidine Autokinase CheA with Its Substrate CheYSolution Structure of the IIAChitobiose-HPr Complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase SystemNew molecular interaction of IIA(Ntr) and HPr from Burkholderia pseudomallei identified by X-ray crystallography and docking studiesStructural biology by NMR: structure, dynamics, and interactions.Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Visualization of transient encounter complexes in protein-protein association.Intramolecular domain-domain association/dissociation and phosphoryl transfer in the mannitol transporter of Escherichia coli are not coupledNovel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent dihydroxyacetone kinase system connected to the pentose phosphate pathwayHow phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteriaImpact of phosphorylation on structure and thermodynamics of the interaction between the N-terminal domain of enzyme I and the histidine phosphocarrier protein of the bacterial phosphotransferase systemStructural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton densityReplica exchange simulations of transient encounter complexes in protein-protein association.Application of NMR methods to the study of the interaction of natural products with biomolecular receptors.Carbohydrate-protein interactions: a 3D view by NMR.Genetic dissection of specificity determinants in the interaction of HPr with enzymes II of the bacterial phosphoenolpyruvate:sugar phosphotransferase system in Escherichia coli.Streptococci and lactococci synthesize large amounts of HPr(Ser-P)(His~P).Solution structure of a post-transition state analog of the phosphotransfer reaction between the A and B cytoplasmic domains of the mannitol transporter IIMannitol of the Escherichia coli phosphotransferase system.Structural basis for the sequestration of the anti-σ(70) factor Rsd from σ(70) by the histidine-containing phosphocarrier protein HPr.Active site phosphoryl groups in the biphosphorylated phosphotransferase complex reveal dynamics in a millisecond time scale.
P2860
Q24311338-98263995-8B1E-4047-9D4A-AA7127A1B28AQ27649838-AEB800F7-00DE-4AAB-A5CB-CFCE18A41710Q27652689-202853D4-35B1-4CA8-A16E-EE89773F7866Q27658430-E6302674-321B-4677-B030-A7B7A52E40B4Q27678432-0A979FD7-55BE-4D71-9329-96D15C15E21CQ27678458-11408644-C2E3-43E5-BD69-C66DA08F2AF6Q27679135-C26BDCBA-D7CD-4D99-AF63-D0A7B28E45B2Q27684162-58D888E1-1EBD-4023-B827-AF47388521C1Q30372281-7A4F6852-F0E6-4A2D-924A-602CCD87BCBCQ33671554-BA13412A-10CE-47B5-B072-4CB2C06CF642Q34038287-272DF0BA-0F8E-4762-A77F-B5C804F05EA6Q34575140-D974B14D-8191-47B4-B9BB-6041E8D94ADCQ35652508-7B7B3EF3-5A40-421B-A93D-7553DC6A65C1Q36197581-19E68436-D03B-422D-B6C2-10F1EDB77172Q36678721-3B721FCC-4C32-494F-A712-FBE62BEB64F9Q36739574-6912684A-E6B1-4B58-AE86-3F397D4E8225Q36797327-DFC64750-B137-413F-8C89-1DFC07B2E323Q36861690-1CD3FBE3-87A8-4F5A-A328-8A1E97C0BF14Q37864564-E167DD7B-3ECF-405E-91FE-BEA14213EED5Q37866236-3560B68C-4535-426A-B6CE-D28BEBCB9801Q42617698-2C465AC4-6C5F-4CD0-B77E-C0B2F7DB23A7Q43473082-471B6BFC-AB73-4CAE-AD5A-41623DC37FF7Q46917261-4D076600-FCAC-48D7-8709-84AABD40BFDEQ54258947-6D94F282-9483-45CF-9268-592806B6ADC7Q54506248-C7FD9DD1-7CE0-46F9-B8D5-0F3F580C422B
P2860
Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system
description
2005 nî lūn-bûn
@nan
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մարտին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Solution NMR structure of the ...... nose phosphotransferase system
@ast
Solution NMR structure of the ...... nose phosphotransferase system
@en
Solution NMR structure of the ...... nose phosphotransferase system
@nl
type
label
Solution NMR structure of the ...... nose phosphotransferase system
@ast
Solution NMR structure of the ...... nose phosphotransferase system
@en
Solution NMR structure of the ...... nose phosphotransferase system
@nl
prefLabel
Solution NMR structure of the ...... nose phosphotransferase system
@ast
Solution NMR structure of the ...... nose phosphotransferase system
@en
Solution NMR structure of the ...... nose phosphotransferase system
@nl
P2093
P2860
P356
P1476
Solution NMR structure of the ...... nose phosphotransferase system
@en
P2093
Alan Peterkofsky
David C Williams
Jeong-Yong Suh
Mengli Cai
P2860
P304
20775-20784
P356
10.1074/JBC.M501986200
P407
P577
2005-03-23T00:00:00Z