@article {976,
	title = {Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces},
	journal = {Journal of Molecular Biology},
	volume = {341},
	number = {1},
	year = {2004},
	note = {ISI Document Delivery No.: 841JCTimes Cited: 25Cited Reference Count: 65},
	month = {Jul},
	pages = {37-54},
	type = {Article},
	abstract = {S1 domains occur in four of the major enzymes of mRNA decay in Escherichia coli: RNase E, PNPase, RNase II, and RNase G. Here, we report the structure of the S1 domain of RNase E, determined by both X-ray crystallography and NMR spectroscopy. The RNase E S1 domain adopts an OB-fold, very similar to that found with PNPase and the major cold shock proteins, in which flexible loops are appended to a well-ordered five-stranded beta-barrel core. Within the crystal lattice, the protein forms a dimer stabilized primarily by intermolecular hydrophobic packing. Consistent with this observation, light-scattering, chemical crosslinking, and NMR spectroscopic measurements confirm that the isolated RNase E S1 domain undergoes a specific monomer-dimer equilibrium in solution with a K-D value in the millimolar range. The substitution of glycine 66 with serine dramatically destabilizes the folded structure of this domain, thereby providing an explanation for the temperature-sensitive phenotype associated with this mutation in full-length RNase E. Based on amide chemical shift perturbation mapping, the binding surface for a single-stranded DNA dodecamer (K-D = 160(+/-40) muM) was identified as a groove of positive electrostatic potential containing several exposed aromatic side-chains. This surface, which corresponds to the conserved ligand-binding cleft found in numerous OB-fold proteins, lies distal to the dimerization interface, such that two independent oligonucleotide-binding sites can exist in the dimeric form of the RNase E S1 domain. Based on these data, we propose that the S1 domain serves a dual role of dimerization to aid in the formation of the tetrameric quaternary structure of RNase E as described by Callaghan et al. in 2003 and of substrate binding to facilitate RNA hydrolysis by the adjacent catalytic domains within this multimeric enzyme. (C) 2004 Elsevier Ltd. All rights reserved.},
	keywords = {BACILLUS-SUBTILIS, C-13-LABELED PROTEINS, CELLULOMONAS-FIMI, CENC, CHEMICAL-SHIFT, COLD-SHOCK PROTEIN, ESCHERICHIA-COLI, MACROMOLECULAR STRUCTURES, MESSENGER-RNA, OB-fold, protein structure, RNA binding, RNase E, ROTATIONAL DIFFUSION, S1 domain, SELECTIVE H-1-N-15 CORRELATIONS},
	isbn = {0022-2836},
	url = {<Go to ISI>://000222925100005},
	author = {Schubert, M. and Edge, R. E. and Lario, P. and Cook, M. A. and Strynadka, N. C. J. and Mackie, G. A. and McIntosh, L. P.}
}
@article {496,
	title = {Site-specific characterization of the association of xylooligosaccharides with the CBM13 lectin-like xylan binding domain from Streptomyces lividans xylanase 10A by NMR spectroscopy},
	journal = {Biochemistry},
	volume = {41},
	number = {13},
	year = {2002},
	note = {ISI Document Delivery No.: 538ARTimes Cited: 12Cited Reference Count: 53},
	month = {Apr},
	pages = {4255-4263},
	type = {Article},
	abstract = {Endo-beta-1,4-xylanase 10A (Xyn10A) from Streptomyces lividans includes an N-terminal catalytic module and a 130-residue C-terminal family 13 carbohydrate-binding module (CBM13). This latter domain adopts a beta-trefoil structure with three potential binding sites (alpha, beta, and gamma) for a variety of small sugars, xylooligosaccharides, and xylan polymers. To investigate the role of this multivalency in carbohydrate binding, we have used NMR spectroscopy to characterize the interaction of isolated CBM13 with a series of sugars. We have assigned resonances from the main chain nuclei of CBM13 using heteronuclear NMR experiments. Analysis of N-15 NMR relaxation data using the extended model free formalism reveals that CBM13 tumbles as an oblate ellipsoid (D-\/D-perpendicular to = 0.80+/-0.02) and that its backbone is relatively rigid on the sub-nanosecond time scale. In particular, the three binding sites show no distinct patterns of increased internal mobility. Ligand-induced chemical shift changes in the H-1-N-15 HSQC spectra of CBM13 were monitored as a function of increasing concentrations Of L-arabinose, lactose, D-xylose, xylobiose, xylotetraose, and xylohexaose. Patterns of shift perturbations for well-resolved resonances demonstrate that all of these sugars associate independently with the three binding sites of CBM13. On the basis of the site-specific association constants derived from a quantitative analysis of these titration data, we show that L-arabinose, lactose, and D-xylose preferentially bind to the alpha site of CBM13, xylobiose binds equally well to all three sites, and xylotetraose and xylohexaose prefer binding to the beta site. Inspection of the crystallographic structure of CBM13 [Notenboom, V., Boraston, A. B., Williams, S. J., Kilburn, D. G., and Rose, D. R. (2002) Biochemistry 41, 4246-4254] provides a rationalization for these results.},
	keywords = {BACKBONE DYNAMICS, CELLULOMONAS-FIMI CENC, CHEMICAL-SHIFTS, CRYSTAL-STRUCTURES, E-86, IMPROVED SENSITIVITY, INSOLUBLE LIGANDS, LIGAND SPECIFICITY, NUCLEAR-MAGNETIC-RESONANCE, OLIVACEOVIRIDIS, ROTATIONAL DIFFUSION},
	isbn = {0006-2960},
	url = {<Go to ISI>://000174792300010},
	author = {Scharpf, M. and Connelly, G. P. and Lee, G. M. and Boraston, A. B. and Warren, R. A. J. and McIntosh, L. P.}
}
@article {4523,
	title = {Can global target analysis of the splitting and spin relaxation from a ring-deuterated mesogen produce dynamical information?},
	journal = {Molecular Crystals and Liquid Crystals Science and Technology Section a-Molecular Crystals and Liquid Crystals},
	volume = {331},
	year = {1999},
	note = {ISI Document Delivery No.: 241JCTimes Cited: 0Cited Reference Count: 2017th International Liquid Crystal ConferenceJUL 19-24, 1998STRASBOURG, FRANCECaisse Epargne, CNRS, Conseil Gen Bas Rhin, France Telecom, Gordon \& Breach Publishing Grp, Instec Inc, Inst Phys Chimie Materiaux Strasbourg, Reg ALSACE, Rolic Liquid Crystals R\&D Co, STOE \& CIE GmbH, Univ Louis Pasteur, Ville Strasbourg, Int Liquid Crystal Soc, Ecole Chimie, Polymeres Materiaux Strasbourg, Lab Fluides Complexex, Inst Charles SadronPart 4},
	pages = {2003-2013},
	type = {Proceedings Paper},
	abstract = {We report on the measurements of quadrupolar splitting and spectral densities of motion for the phenylthio ring deuterons as a function of temperature in 4-pentylphenylthio-4{\textquoteright}-octyloxy- benzoate ((8) over bar S5 - d(4)). A global analysis of all these observables at 9 different temperatures in the nematic and smectic A phases is shown to give useful information on the core dynamics of (8) over bar S5. Inclusion of the smectic C phase in the global analysis is possible; but gives a poorer overall fitting quality factor.},
	keywords = {deuteron spin relaxation, LIQUID-CRYSTAL PHASES, MOLECULAR ORDER, MOTIONS, NMR, RESONANCE, ROTATIONAL DIFFUSION, smectogen},
	isbn = {1058-725X},
	url = {<Go to ISI>://000082878400020},
	author = {Dong, R. Y. and Bates, G. S. and Shen, X.}
}
