Journal ArticleDOI
Predicting coiled coils from protein sequences
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TLDR
This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled -coil structures,such as the hinge region in myosin.Abstract:
The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.read more
Citations
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The rad18 gene of Schizosaccharomyces pombe defines a new subgroup of the SMC superfamily involved in DNA repair.
Alan R. Lehmann,M Walicka,Dominic J. F. Griffiths,Johanne M. Murray,Felicity Z. Watts,S. Mccready,Antony M. Carr +6 more
TL;DR: Gene deletion shows that both rad18 and RHC18 are essential for proliferation and suggests that the product of the rad18 gene acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair.
Journal ArticleDOI
Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis.
Dennis Claessen,Robyn Emmins,Leendert W. Hamoen,Richard A. Daniel,Jeff Errington,David H. Edwards +5 more
TL;DR: This work identifies the cell division protein, EzrA, and a newly discovered protein, GpsB, as key players in the elongation–division cycle of Bacillus subtilis, and shows that these phenotypes are tightly associated with disturbed localization of the major transglycosylase/transpeptidase of the cell, PBP1.
Journal ArticleDOI
Positionally Cloned Human Disease Genes: Patterns of Evolutionary Conservation and Functional Motifs
TL;DR: Comparisons to complete sequence databases and to separate databases of nematode, yeast, and bacterial proteins showed that for most of the disease gene products, statistically significant sequence similarities are detectable in each of the model organisms.
Journal ArticleDOI
Midbody Targeting of the ESCRT Machinery by a Noncanonical Coiled Coil in CEP55
TL;DR: In this paper, the crystal structure of the EABR bound to an ALIX peptide at a resolution of 2.0 angstroms was solved, and it was shown that the structure formed an aberrant dimeric parallel coiled coil.
Journal ArticleDOI
Predicting coiled-coil regions in proteins.
TL;DR: Several widely noted predictions, among them those for heterotrimeric G proteins and for cartilage oligomeric matrix protein, have been confirmed by crystal structures, and several new predictions have been made, including a model for the still hypothetical right-handed coiled coil.
References
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Journal ArticleDOI
The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins
TL;DR: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein, and may represent a characteristic property of a new category of DNA binding proteins.
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Evidence that the leucine zipper is a coiled coil
TL;DR: A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and characterized and associates in the micromolar concentration range to form a very stable dimer of alpha helices with a parallel orientation.
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Cyclic AMP-responsive DNA-binding protein: structure based on a cloned placental cDNA.
TL;DR: The putative DNA-binding domain of CREB is structurally similar to the corresponding domains in the phorbol ester-responsive c-jun protein and the yeast transcription factor GCN4.
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α‐Helical coiled coils and bundles: How to design an α‐helical protein
Carolyn Cohen,David A.D. Parry +1 more
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A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
TL;DR: The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 Å resolution, is described, and is the first representative of a second class of aminoacyl-tRNA synthet enzyme structures.