Related ArticlesHigh precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division.
J Mol Biol. 2000 Nov 24;304(2):219-29
Authors: Katoh E, Hatta T, Shindo H, Ishii Y, Yamada H, Mizuno T, Yamazaki T
YhhP, a small protein of 81 amino acid residues encoded by the yhhP gene in the Escherichia coli database, is implicated in cell division although the precise biological function of this protein has not been yet identified. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. We have determined the three-dimensional solution structure of YhhP by NMR spectroscopy in order to obtain insight into its biological function. It folds into a two-layered alpha/beta-sandwich structure with a betaalphabetaalphabetabeta fold, comprising a mixed four-stranded beta-sheet stacked against two alpha-helices, both of which are nearly parallel to the strands of the beta-sheet. The CPxP motif plays a significant structural role in stabilizing the first helix as a part of the new type N-capping box where the Cys-Pro peptide bond adopts a cis configuration. The structure of YhhP displays a striking resemblance to the C-terminal ribosome-binding domain of translation initiation factor IF3 (IF3C). In addition, the surface charge distribution of the RNA-recognition helix of IF3C is nearly the same as that of the corresponding helix of YhhP. These results suggest a structure-based hypothesis in which binding to an RNA target plays an essential role in the function of this ubiquitous protein.
[NMR paper] High precision NMR structure and function of the RING-H2 finger domain of EL5, a rice
High precision NMR structure and function of the RING-H2 finger domain of EL5, a rice protein whose expression is increased upon exposure to pathogen-derived oligosaccharides.
Related Articles High precision NMR structure and function of the RING-H2 finger domain of EL5, a rice protein whose expression is increased upon exposure to pathogen-derived oligosaccharides.
J Biol Chem. 2003 Apr 25;278(17):15341-8
Authors: Katoh S, Hong C, Tsunoda Y, Murata K, Takai R, Minami E, Yamazaki T, Katoh E
EL5, a RING-H2 finger protein, is rapidly induced by...
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[NMR paper] NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zin
NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins.
Related Articles NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins.
Proteins. 2002 Nov 1;49(2):289-93
Authors: Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA
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[NMR paper] High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli d
High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase.
Related Articles High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase.
Biochemistry. 2000 Oct 24;39(42):12789-95
Authors: Kitahara R, Sareth S, Yamada H, Ohmae E, Gekko K, Akasaka K
A high-pressure (15)N/(1)H two-dimensional NMR study has been carried out on folate-bound dihydrofolate reductase (DHFR) from Escherichia coli in the pressure range between 30 and 2000 bar. Several...
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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] The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general
The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
Related Articles The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
EMBO J. 1998 Nov 2;17(21):6377-84
Authors: Stoldt M, Wöhnert J, Görlach M, Brown LR
The structure of the Escherichia coli ribosomal protein L25 has been determined to an r.m.s. displacement of backbone heavy atoms of 0.62 +/- 0.14 A by multi-dimensional...
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[NMR paper] Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli:
Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
Proc Natl Acad Sci U S A. 1994 May 24;91(11):5114-8
Authors: Newkirk K, Feng W, Jiang W, Tejero R, Emerson SD, Inouye M, Montelione GT
Sequence-specific...
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[NMR paper] Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli:
Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.
Proc Natl Acad Sci U S A. 1994 May 24;91(11):5114-8
Authors: Newkirk K, Feng W, Jiang W, Tejero R, Emerson SD, Inouye M, Montelione GT
Sequence-specific...
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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...