Related ArticlesNMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.
Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11343-7
Authors: Szyperski T, Pellecchia M, Wall D, Georgopoulos C, Wüthrich K
DnaJ from Escherichia coli is a 376-amino acid protein that functions in conjunction with DnaK and GrpE as a chaperone machine. The N-terminal fragment of residues 2-108, DnaJ-(2-108), retains many of the activities of the full-length protein and contains a structural motif, the J domain of residues 2-72, which is highly conserved in a superfamily of proteins. In this paper, NMR spectroscopy was used to determine the secondary structure and the three-dimensional polypeptide backbone fold of DnaJ-(2-108). By using 13C/15N doubly labeled DnaJ-(2-108), nearly complete sequence-specific assignments were obtained for 1H, 15N, 13C alpha, and 13C beta, and about 40% of the peripheral aliphatic carbon resonances were also assigned. Four alpha-helices in polypeptide segments of residues 6-11, 18-31, 41-55, and 61-68 in the J domain were identified by sequential and medium-range nuclear Overhauser effects. For the J domain, the three-dimensional structure was calculated with the program DIANA from an input of 536 nuclear Overhauser effect upper-distance constraints and 52 spin-spin coupling constants. The polypeptide backbone fold is characterized by the formation of an antiparallel bundle of two long helices, residues 18-31 and 41-55, which is stabilized by a hydrophobic core of side chains that are highly conserved in homologous J domain sequences. The Gly/Phe-rich region from residues 77 to 108 is flexibly disordered in solution.
[NMR paper] Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli m
Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system.
Related Articles Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the Escherichia coli mannose phosphotransferase system.
J Biol Chem. 2005 May 27;280(21):20775-84
Authors: Williams DC, Cai M, Suh JY, Peterkofsky A, Clore GM
The solution structure of the 48-kDa IIA(Man)-HPr complex of the mannose branch of the Escherichia coli phosphotransferase system has been solved by NMR using conjoined rigid body/torsion...
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[NMR paper] NMR structure of ribonuclease HI from Escherichia coli.
NMR structure of ribonuclease HI from Escherichia coli.
Related Articles NMR structure of ribonuclease HI from Escherichia coli.
Biol Pharm Bull. 2000 Oct;23(10):1147-52
Authors: Fujiwara M, Kato T, Yamazaki T, Yamasaki K, Nagayam K
The solution structure of ribonuclease HI (RNase HI) from Escherichia coli (E. coli), a protein of 155 residues, was determined. Three-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain 1,424 distance constraints between individually assigned polypeptide chain hydrogen atoms....
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[NMR paper] Studies on the NusB protein of Escherichia coli--expression and determination of seco
Studies on the NusB protein of Escherichia coli--expression and determination of secondary-structure elements by multinuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Studies on the NusB protein of Escherichia coli--expression and determination of secondary-structure elements by multinuclear NMR spectroscopy.
Eur J Biochem. 1997 Sep 1;248(2):338-46
Authors: Berglechner F, Richter G, Fischer M, Bacher A, Gschwind RM,...
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[NMR paper] NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli Dna
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
J Mol Biol. 1996 Jul 12;260(2):236-50
Authors: Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K
The recombinant N-terminal 107-amino acid polypeptide fragment 2-108 of the DnaJ molecular chaperone of Escherichia...
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[NMR paper] 1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli
1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein.
Eur J Biochem. 1993 Aug 1;215(3):573-85
Authors: Bruix M, Pascual J, Santoro J, Prieto J, Serrano L, Rico M
Che Y is a 129-residue parallel alpha/beta protein involved in bacterial...
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[NMR paper] The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli pho
The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.
FEBS Lett. 1993 Jan 2;315(1):11-5
Authors: van Nuland NA, Kroon GJ, Dijkstra K, Wolters GK, Scheek RM, Robillard GT
The region of the surface of...
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[NMR paper] NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. c
NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Protein Sci. 1992...
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[NMR paper] 1H NMR study of the solution molecular and electronic structure of Escherichia coli f
1H NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: evidence for S = 1/2 in equilibrium S = 5/2 spin equilibrium for intact His/Met ligation.
Related Articles 1H NMR study of the solution molecular and electronic structure of Escherichia coli ferricytochrome b562: evidence for S = 1/2 in equilibrium S = 5/2 spin equilibrium for intact His/Met ligation.
Biochemistry. 1991 Feb 26;30(8):2156-65
Authors: Wu JZ, La Mar GN, Yu LP, Lee KB, Walker FA, Chiu ML, Sligar SG
The solution 500-MHz 1H NMR...