@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 {4312,
	title = {Equus caballus gelsolin - cDNA sequence and protein structural implications},
	journal = {European Journal of Biochemistry},
	volume = {251},
	number = {3},
	year = {1998},
	note = {ISI Document Delivery No.: YV719Times Cited: 4Cited Reference Count: 48},
	month = {Feb},
	pages = {613-621},
	type = {Article},
	abstract = {We have generated and characterized the cDNA from equine smooth muscle that Encodes gelsolin, an actin-modulating protein. Overlapping cDNA clones synthesized by the reverse transcriptaseoplymerase chain reaction and clones isolated from a horse genomic library provided the complete primary structure for the intracellular isoform of gelsolin, while cDNA complemented with protein sequence data produced the full-length primary transcript of the gelsolin isoform found circulating in equine plasma. The deduced amino acid sequences of the intracellular and secreted versions of equine gelsolin infer polypeptides of 731 and 755 residues with apparent molecular masses of 80.7 kDa and 83.2 kDa, respectively. Multiple sequence alignment analysis of equine, human, porcine, and murine orthologs of gelsolin demonstrates prominent similarities among all of these proteins, with the horse and human molecules exhibiting the largest degree of likeness with respect to polypeptide length and overall sequence composition. Both horse and human plasma gelsolins are comprised of 755 amino acids with 94\% of the residues identical, while the degree of sequence identity in the shorter (731 residues) cytoplasmic gelsolins is 95 \%. Analysis of the sequences and structures of the six related domains that comprise gelsolin emphasizes the strong correlation that exists between primary structural conservation among mammalian gelsolins and maintenance of the three-dimensional domain fold characteristic of members of this protein family.},
	keywords = {actin-binding protein, ACTIN-SEVERING PROTEINS, amino acid sequence, AMPLIFICATION, BINDING DOMAIN, cDNA sequence, CLONING, CYTOPLASMIC FORMS, DNA, END, extraction, gelsolin, HORSE PLASMA GELSOLIN, MUSCLE, protein structure},
	isbn = {0014-2956},
	url = {<Go to ISI>://000071855900009},
	author = {Koepf, E. K. and Hewitt, J. and Vo, H. and MacGillivray, R. T. A. and Burtnick, L. D.}
}
@article {3819,
	title = {Structural coupling of the inhibitory regions flanking the ETS domain of murine Ets-1},
	journal = {Protein Science},
	volume = {5},
	number = {2},
	year = {1996},
	note = {ISI Document Delivery No.: TU724Times Cited: 46Cited Reference Count: 66},
	month = {Feb},
	pages = {296-309},
	type = {Article},
	abstract = {Several members of the ets gene family of transcription factors show negative regulation of DNA binding by intramolecular interactions. A structural mechanism for this auto-inhibition is investigated using a 161-residue N-terminal deletion mutant of murine Ets-1, Ets-1 Delta N280. This protein shows a similar reduced affinity for DNA as native Ets-1 because it contains the ETS domain in context of the flanking amino- and carboxy-terminal regions that together mediate repression of DNA binding. The secondary structure of Ets-1 Delta N280 was determined using NMR chemical shift, NOE, J coupling, and amide hydrogen exchange information. In addition to the winged helix-turn-helix ETS domain, Ets-1 Delta N280 contains two alpha-helices in the amino-terminal inhibitory region and one alpha-helix in the carboxy-terminal inhibitory region. Chemical shift comparisons were made between this protein and an activated form of Ets-1 lacking the amino-terminal inhibitory region. The spectral differences demonstrate that the amino- and carboxy-terminal inhibitory sequences are structurally coupled to one another, thus explaining the observation that both regions are required for the repression of DNA binding. Furthermore, these data show that the inhibitory sequences also interact directly with the first helix of the intervening ETS domain, thereby providing a pathway for the repression of DNA binding. These results lead to a model of an inhibitory module in Ets-1 composed of both the amino- and carboxy-terminal regions interfaced with the ETS domain. This establishes the structural framework for understanding the intramolecular inhibition of Ets-1 DNA binding.},
	keywords = {3-DIMENSIONAL NMR-SPECTROSCOPY, allosteric, ASSIGNMENT, CRYSTAL-STRUCTURE, DNA binding, DNA-BINDING MOTIF, ETS domain, Ets-1 and Ets-2, FACTORS, H-1, INHIBITION, INTRAMOLECULAR, LARGER PROTEINS, N-15 NMR, NMR, protein structure, SPECTRA, transcription, V-ETS, winged helix-turn-helix},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1996TU72400014},
	author = {Skalicky, J. J. and Donaldson, L. W. and Petersen, J. M. and Graves, B. J. and McIntosh, L. P.}
}
