@article {934,
	title = {Diversity in structure and function of the Ets family PNT domains},
	journal = {Journal of Molecular Biology},
	volume = {342},
	number = {4},
	year = {2004},
	note = {ISI Document Delivery No.: 855WLTimes Cited: 17Cited Reference Count: 86},
	month = {Sep},
	pages = {1249-1264},
	type = {Article},
	abstract = {The PNT (or Pointed) domain, present within a subset of the Ets family of transcription factors, is structurally related to the larger group of SAM domains through a common tertiary arrangement of four alpha-helices. Previous studies have shown that, in contrast to the PNT. domain from Tel, this domain from Ets-1 contains an additional N-terminal helix integral to its folded structure. To further investigate the structural plasticity of the PNT domain, we have used NMR spectroscopy to characterize this domain from two additional Ets proteins, Erg and GABPalpha. These studies both define the conserved and variable features of the PNT domain, and demonstrate that the additional N-terminal helix is also present in GABPa, but not Erg. In contrast to Tel and Yan, which self-associate to form insoluble polymers, we also show that the isolated PNT domains from Ets-1, Ets-2, Erg, Fli-1, GABPalpha, and Pnt-P2 are monomeric in solution. Furthermore, these soluble PNT domains do not associate in any pair-wise combination. Thus these latter Ets family PNT domains likely mediate interactions with additional components of the cellular signaling or transcriptional machinery. (C) 2004 Elsevier Ltd. All rights reserved.},
	keywords = {ALPHA-MOTIF SAM, ASSIGNMENT, AUTOMATED, CHEMICAL-SHIFT, DIPOLAR COUPLINGS, ENDOTHELIAL-CELL DIFFERENTIATION, Erg, GABP, GENE, NMR-SPECTRA, POINTED DOMAIN, protein interactions, PROTEIN-KINASE, SAM domain, TRANSCRIPTION FACTOR},
	isbn = {0022-2836},
	url = {<Go to ISI>://000224005500015},
	author = {Mackereth, C. D. and Scharpf, M. and Gentile, L. N. and Macintosh, S. E. and Slupsky, C. M. and McIntosh, L. P.}
}
@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 {4745,
	title = {Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C},
	journal = {Biochemistry},
	volume = {39},
	number = {10},
	year = {2000},
	note = {ISI Document Delivery No.: 294HFTimes Cited: 31Cited Reference Count: 74},
	month = {Mar},
	pages = {2445-2458},
	type = {Article},
	abstract = {The 1,4-beta-glucanase CenC from Cellulomonas fimi contains two cellulose-binding domains, CBDN1 and CBDN2, arranged in tandem at its N-terminus. These homologous CBDs are distinct in their selectivity for binding amorphous and not crystalline cellulose. Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of CBDN2 in the presence of saturating amounts of cellopentaose. A total of 1996 experimental restraints were used to calculate an ensemble of 21 final structures for the protein. CBDN2 is composed of 11 beta-strands, folded into two antiparallel beta-sheets, with a topology of a jellyroll beta-sandwich. On the basis of patterns of chemical shift perturbations accompanying the addition of cellooligosaccharides, as well as the observation of intermolecular protein-sugar NOE interactions, the cellulose-binding site of CBDN2 was identified as a cleft that lies across one face of the beta-sandwich. The thermodynamic basis for the binding of cellooligosaccharides was investigated using isothermal titration calorimetry and NMR spectroscopy. Binding is enthalpically driven and consistent with a structural model involving hydrogen bonding between the equatorial hydroxyls of the glucopyranosyl rings and polar amino acid side chains lining the CBDN2 cleft. Affinity electrophoresis was used to determine that CBDN2 also binds soluble beta-1,4-linked polymers of glucose, including hydroxyethylcellulose and beta-1,3-1,4-glucans. This study complements a previous analysis of CBDN1 [Johnson, P. E., Joshi, M. D., Tomme, P., Kilburn, D. G., and McIntosh, L. P. (1996) Biochemistry 35, 14381-14394] and demonstrates that the homologous CBDs from CenC share very similar structures and sugar binding properties.},
	keywords = {3-DIMENSIONAL SOLUTION STRUCTURE, C-13-ENRICHED PROTEINS, C-13-LABELED PROTEINS, CHEMICAL-SHIFT, DISTANCE GEOMETRY, IMPROVED SENSITIVITY, INDEX, ISOTOPICALLY-ENRICHED PROTEINS, LARGER PROTEINS, NUCLEAR-MAGNETIC-RESONANCE, SIDE-CHAIN RESONANCES},
	isbn = {0006-2960},
	url = {<Go to ISI>://000085905300003},
	author = {Brun, E. and Johnson, P. E. and Creagh, A. L. and Tomme, P. and Webster, P. and Haynes, C. A. and McIntosh, L. P.}
}
@article {3707,
	title = {Structure of the N-terminal cellulose-binding domain of Cellulomonas fimi CenC determined by nuclear magnetic resonance spectroscopy},
	journal = {Biochemistry},
	volume = {35},
	number = {45},
	year = {1996},
	note = {ISI Document Delivery No.: VT081Times Cited: 94Cited Reference Count: 90},
	month = {Nov},
	pages = {14381-14394},
	type = {Article},
	abstract = {Multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy was used to determine the tertiary structure of the 152 amino acid N-terminal cellulose-binding domain from Cellulomonas fimi 1,4-beta-glucanase CenC (CBDN1) CBDN1 was studied in the presence of saturating concentrations of cellotetraose, but due to spectral overlap, the oligosaccharide was not included in the structure calculations. A total of 1705 interproton nuclear Overhauser effect (NOE), 56 phi, 88 psi, 42 chi 1, 9 chi 2 dihedral angle, and 88 hydrogen-bond restraints were used to calculate 25 final structures. These structures have a rmsd from the average of 0.79 +/- 0.11 Angstrom for all backbone atoms excluding disordered termini and 0.44 +/- 0.05 Angstrom for residues with regular secondary structures. CBDN1 is composed of 10 beta-strands, folded into two antiparallel beta-sheets with the topology of a jelly-roll beta-sandwich. The strands forming the face of the protein previously determined by chemical shift perturbations to be responsible for cellooligosaccharide binding [Johnson, P. E., Tomme, P., Joshi, M. D., \& McIntosh, L. P. (1996) Biochemistry, 35, 13895-13906] are shorter than those forming the opposite side of the protein. This results in a 5-stranded binding cleft, containing a central strip of hydrophobic residues that is flanked on both sides by polar hydrogen-bonding groups. The presence of this cleft provides a structural explanation for the unique selectivity of CBDN1 for amorphous cellulose and other soluble oligosaccharides and the lack of binding to crystalline cellulose, The tertiary structure of CBDN1 is strikingly similar to that of the bacterial 1,3-1,4-beta-glucanases, as well as other sugar-binding proteins with jelly-roll folds.},
	keywords = {3-DIMENSIONAL SOLUTION STRUCTURE, C-13-ENRICHED PROTEINS, CHEMICAL-SHIFT, DISTANCE GEOMETRY, INDEX, ISOTOPICALLY-ENRICHED PROTEINS, LARGER PROTEINS, NMR-SPECTROSCOPY, REESEI CELLOBIOHYDROLASE-I, SIDE-CHAIN RESONANCES, TRICHODERMA-REESEI},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1996VT08100039},
	author = {Johnson, P. E. and Joshi, M. D. and Tomme, P. and Kilburn, D. G. and McIntosh, L. P.}
}
