About: The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 01 January 1993

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1993 (uk) article scientifique publié en 1993 (fr) im Januar 1993 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 1993 (ast) artikull shkencor i botuar më 01 janar 1993 (sq) scientific article published on 01 January 1993 (en)
publication date	wds:Q70521457-A9832220-C8DA-42A2-88C2-FD07C17C3A49
publication date	1993-01-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q70521457-9CD01F4F-C9E8-4362-9115-FE48305EA807
language of work or name	English
cites work	wds:Q70521457-42B6F66C-F555-4EE7-9FD9-BE514B94365C wds:Q70521457-5100117B-DA50-4A30-9644-057A1CD2DAFC wds:Q70521457-97ECF79E-A109-4BD6-8670-300E9B1270EF wds:Q70521457-98E14442-9504-49B4-AA84-A8DF7EE630BA wds:Q70521457-C623C4F6-D131-44D2-82F7-2B1EC3191795 wds:Q70521457-DA07F16B-424D-4410-91EA-DE20CC440ED6 wds:Q70521457-DBC73899-9DC5-4FBA-84D6-4A2DCCFDD2E4 wds:Q70521457-E9BCF6CF-52B2-4BCC-86CF-4EEFEE7B5BD7 wds:Q70521457-F1B0A0A1-B964-4244-A971-8CAC9D3B6036 wds:Q70521457-F789ED84-17BD-481B-9BD6-42367A84E646
cites work	Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution Phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli: overexpression, purification, and characterization of the enzymatically active C-terminal domain of enzyme IImtl equivalent to enzyme IIImtl Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap Exchange of phosphoryl groups between HPr molecules of the phosphoenolpyruvate-dependent phosphotransferase system is an autocatalytic process Two-dimensional 1H NMR studies of histidine-containing protein from Escherichia coli. 3. Secondary and tertiary structure as determined by NMR. Three-dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli. Assignment of backbone resonances. Enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: protein-protein and protein-phospholipid interactions. Reexamination of the secondary and tertiary structure of histidine-containing protein from Escherichia coli by homonuclear and heteronuclear NMR spectroscopy Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy Characterization of phosphorylated histidine-containing protein (HPr) of the bacterial phosphoenolpyruvate:sugar phosphotransferase system
author name string	wds:Q70521457-19099D8F-2962-4AC3-9F4D-1EF53F11EE42 wds:Q70521457-2F700FE9-BAFE-46B1-A4ED-A6B9E2C8A2B6 wds:Q70521457-76ED5FAC-4128-4AFF-9657-0835C1A4A8C0 wds:Q70521457-9906AE37-6D84-4261-9CD8-3046C9F4C8DB wds:Q70521457-B4301945-2B57-43EF-9456-B30DD9B6E052 wds:Q70521457-D05E5FB8-DD49-46B8-92B2-CB0BFBDA576E
author name string	G T Robillard K Dijkstra R M Scheek N A van Nuland G J Kroon G K Wolters
rdfs:label	The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system (en) The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system (sq) The NMR determination of the IIA (nl)
skos:prefLabel	The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system (en) The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system (sq) The NMR determination of the IIA (nl)
name	The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system (en) The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system (sq) The NMR determination of the IIA (nl)
title	wds:Q70521457-E9A004DD-9528-4D41-A395-4B263A6819CC
title	The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system (en)
page(s)	wds:Q70521457-09CDA898-78F6-49BD-B174-6A22872BA2C4
page(s)	11-15
instance of	wds:Q70521457-4CC48C35-D6D2-4A84-A4FB-61CA463BD8B2
instance of	scholarly article
main subject	wds:Q70521457-F0183107-CBB5-43B2-BD83-808163C4E4D5
main subject	Escherichia coli
PubMed ID	wds:Q70521457-3666AF19-DC57-4320-A03C-4C2C001496AF
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8416803
PubMed ID	8416803
published in	wds:Q70521457-C5E23B6C-E634-4C9F-88E6-14CFE47E74EC
published in	FEBS Letters
issue	wds:Q70521457-32F81D56-617C-4A4F-9076-394B98F432F6
volume	wds:Q70521457-1032A799-E9E4-4FE8-B09D-E3F1B37F89C9
issue	1
volume	315
number of pages	wds:Q70521457-A16466AB-DEC3-4B15-84CA-26A16F8AB23F
number of pages	5 (xsd:decimal)
DOI	wds:Q70521457-A300E428-AC30-48C1-A934-230D91C209EB
DOI	http://dx.doi.org/10.1016/0014-5793(93)81122-G
DOI	10.1016/0014-5793(93)81122-G
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q70521457
is cites work of	A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase system A common interface on histidine-containing phosphocarrier protein for interaction with its partner proteins Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr Automated evaluation of chemical shift perturbation spectra: New approaches to quantitative analysis of receptor-ligand interaction NMR spectra The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three-dimensional NMR spectroscopy The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site Interaction between calcium-free calmodulin and IQ motif of neurogranin studied by nuclear magnetic resonance spectroscopy. Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy Antibody variable region binding by Staphylococcal protein A: thermodynamic analysis and location of the Fv binding site on E-domain Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA Structure from NMR and molecular dynamics: Distance restraining inhibits motion in the essential subspace. Demonstration of protein-protein interaction specificity by NMR chemical shift mapping NMR characterization of interleukin-2 in complexes with the IL-2Ralpha receptor component, and with low molecular weight compounds that inhibit the IL-2/IL-Ralpha interaction Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments Identification and characterization of modular domains that bind ubiquitin Structural and biochemical evaluation of the interaction of the phosphatidylinositol 3-kinase p85alpha Src homology 2 domains with phosphoinositides and inositol polyphosphates The solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif
is cites work of	wds:Q27730402-C14A56FB-0B71-4635-984A-996E8DFF2920 wds:Q28828615-1040F37C-6738-4CC4-A748-BE46CBA127CE wds:Q27733395-3E943990-983D-4ED8-B20A-65E78CA855C6

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 196 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software