Thursday, February 8, 2018

Nature Structural & Molecular Biology Contents: 2018 Volume #25 pp 115 - 194

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Nature Structural & Molecular Biology

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February 2018 Volume 25, Issue 2

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Review Articles


Structural insights into the design of novel anti-influenza therapies    pp115 - 121
Nicholas C. Wu & Ian A. Wilson

Wu and Wilson review our structural knowledge of influenza virus HA and broadly neutralizing antibodies, which have opened the way for design of novel vaccines and therapeutics.


The ring-shaped hexameric helicases that function at DNA replication forks    pp122 - 130
Michael E. O'Donnell & Huilin Li

In this Review, the authors discuss our current understanding of how the hexameric helicases that catalyze helix unwinding during DNA replication are physically and functionally integrated with other replisome components.


Brief Communications


Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp    pp131 - 134
Marcus Gallagher-Jones, Calina Glynn, David R. Boyer, Michael W. Martynowycz, Evelyn Hernandez et al.

MicroED structure of a peptide from the β22 loop of the bank vole prion protein reveals a protofibril stabilized by a dense network of hydrogen bonds.


Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex    pp135 - 138


The cryo-EM structure of the human core CPSF complex, containing CPSF160, WDR33, CPSF30 and Fip1 subunits, bound to its RNA target reveals the mechanism of PAS recognition.


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Cryo-EM structure of the exocyst complex    pp139 - 146
Kunrong Mei, Yan Li, Shaoxiao Wang, Guangcan Shao, Jia Wang et al.

The structure of the fully assembled yeast exocyst complex, which mediates the tethering of secretory vesicles to the plasma membrane during exocytosis, provides new insights to hierarchical complex assembly and the mechanism of vesicle tethering.


TRF1 participates in chromosome end protection by averting TRF2-dependent telomeric R loops    pp147 - 153
Yong Woo Lee, Rajika Arora, Harry Wischnewski & Claus M. Azzalin

In vitro and cellular assays unexpectedly reveal that shelterin protein TRF2 binds TERRA and stimulates strand invasion within telomere repeats and that TRF1 suppresses this activity to prevent telomere loss and genome instability.


Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes    pp154 - 162
Simon Poepsel, Vignesh Kasinath & Eva Nogales

Cryo-EM analyses of human PRC2 bound to dinucleosomes with one unmodified (substrate) and one H3K27me3-containing (activating) nucleosome support a model for H3K27me3-based PRC2 activation and spreading.


Solution structure and elevator mechanism of the membrane electron transporter CcdA    pp163 - 169
Yunpeng Zhou & John H. Bushweller

An NMR structure of Thermus thermophilus membrane electron transporter CcdA in an oxidized, outward-facing state suggests an elevator-type mechanism shuttles reactive cysteines to relay reducing equivalents across the membrane.


Structural basis for recognition of diverse antidepressants by the human serotonin transporter    pp170 - 175
Jonathan A. Coleman & Eric Gouaux

The X-ray structures of engineered variants of the human serotonin transporter show that the antidepressants sertraline, fluvoxamine and paroxetine occupy the central substrate-binding site and stabilize the transporter in an outward-open conformation.


Technical Reports


Spatiotemporal allele organization by allele-specific CRISPR live-cell imaging (SNP-CLING)    pp176 - 184
Philipp G. Maass, A. Rasim Barutcu, David M. Shechner, Catherine L. Weiner, Marta Melé et al.

An allele-specific CRISPR-based DNA imaging technique provides insights into allelic positioning in live mouse cells. Spatiotemporal monitoring reveals that allele positions may fluctuate during cell state transitions.


Visualization and analysis of non-covalent contacts using the Protein Contacts Atlas    pp185 - 194
Melis Kayikci, A. J. Venkatakrishnan, James Scott-Brown, Charles N. J. Ravarani, Tilman Flock et al.

The Protein Contacts Atlas is an interactive resource of non-covalent contacts that can generate multiple representations of non-covalent contacts from PDB structures at different scales, from atoms to subunits and entire complexes.


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