Friday, July 13, 2018

Nature Structural & Molecular Biology Contents: 2018 Volume #25 pp 547 - 640

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TABLE OF CONTENTS

July 2018 Volume 25, Issue 7

Obituary
Articles
Resources
 
 
 

Obituary

 

Elisa Izaurralde 1959–2018    p547
Matthias W. Hentze & Juan Valcárcel
doi:10.1038/s41594-018-0081-1

Articles

 

Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states    pp548 - 556
Ahmed-Noor A. Agip, James N. Blaza, Hannah R. Bridges, Carlo Viscomi, Shaun Rawson et al.
doi:10.1038/s41594-018-0073-1

Cryo-EM analyses of mitochondrial complex I (NADH:ubiquinone oxidoreductase) isolated from mouse heart allow comparisons between the active and deactive states and provide new mechanistic insights into this important complex.

 

Structural basis of meiotic chromosome synapsis through SYCP1 self-assembly    pp557 - 569
James M. Dunce, Orla M. Dunne, Matthew Ratcliff, Claudia Millán, Suzanne Madgwick et al.
doi:10.1038/s41594-018-0078-9

The structural basis for self-assembly of human SYCP1, the core architectural element of the meiotic synaptonemal complex, reveals an obligate tetrameric structure that assembles into a zipper-like supramolecular lattice.

 

Crystal structure of the human angiotensin II type 2 receptor bound to an angiotensin II analog    pp570 - 576
Hidetsugu Asada, Shoichiro Horita, Kunio Hirata, Mitsunori Shiroishi, Yuki Shiimura et al.
doi:10.1038/s41594-018-0079-8

The crystal structure of human AT2R binding an angiotensin II analog reveals ‘core’ and ‘extended’ domains within the binding pocket. A signature positively charged motif orients the C terminus of the peptide ligand at the bottom of the binding pocket.

 

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Accurate design of translational output by a neural network model of ribosome distribution    pp577 - 582
Robert Tunney, Nicholas J. McGlincy, Monica E. Graham, Nicki Naddaf, Lior Pachter et al.
doi:10.1038/s41594-018-0080-2

Neural network analyses of ribosome profiling data reveal sequence features that affect translation elongation, which can be manipulated to control protein expression levels in yeast.

 

Structure of the core of the type III secretion system export apparatus    pp583 - 590
Lucas Kuhlen, Patrizia Abrusci, Steven Johnson, Joseph Gault, Justin Deme et al.
doi:10.1038/s41594-018-0086-9

Cryo-EM structure of the Salmonella Typhimurium FliP–FliQ–FliR complex identifies this export gate as a core component of the periplasmic portion of the type III secretion system.

 

Mechanism of 53BP1 activity regulation by RNA-binding TIRR and a designer protein    pp591 - 600
Maria Victoria Botuyan, Gaofeng Cui, Pascal Drané, Catarina Oliveira, Alexandre Detappe et al.
doi:10.1038/s41594-018-0083-z

Structural and functional dissection of the TIRR–53BP1 complex shows that TIRR acts as a regulatory switch that blocks 53BP1 binding to chromatin to direct DNA repair, and it releases 53BP1 in response to DNA damage by binding RNA.

 

A CLC-type F-/H+ antiporter in ion-swapped conformations    pp601 - 606
Nicholas B. Last, Randy B. Stockbridge, Ashley E. Wilson, Tania Shane, Ludmila Kolmakova-Partensky et al.
doi:10.1038/s41594-018-0082-0

Crystal structures of the CLCF proton-coupled fluoride antiporter Eca in two conformations capture two rotamers of the gating glutamate and reveal simultaneous accessibility of F and H+ ions via separate pathways on opposite sides of the membrane.

 

The role of tubulin–tubulin lattice contacts in the mechanism of microtubule dynamic instability    pp607 - 615
Szymon W. Manka & Carolyn A. Moores
doi:10.1038/s41594-018-0087-8

Cryo-EM analyses of microtubules in different nucleotide-bound states reveal differences in lateral and longitudinal contacts within the lattice, indicating the structural basis for microtubule catastrophe.

 

Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1–Npl4    pp616 - 622
Nicholas O. Bodnar, Kelly H. Kim, Zhejian Ji, Thomas E. Wales, Vladimir Svetlov et al.
doi:10.1038/s41594-018-0085-x

Structures of Cdc48 with heterodimeric cofactor Ufd1–Npl4 reveal the location of Npl4's MPN domain above Cdc48’s central pore, thus suggesting how Npl4 engages with polyubiquitinated substrates and promotes their translocation into the ATPase.

 

Mechanism of parkin activation by phosphorylation    pp623 - 630
Véronique Sauvé, George Sung, Naoto Soya, Guennadi Kozlov, Nina Blaimschein et al.
doi:10.1038/s41594-018-0088-7

Crystal structures of activated, phosphorylated fly parkin in complex with phosphorylated ubiquitin and human UbcH7 reveal large domain movements enabled by the parkin’s internal linkers. Results also explain some Parkinson’s disease mutations.

 

Resources

 

UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites    pp631 - 640
Vyacheslav Akimov, Inigo Barrio-Hernandez, Sten V. F. Hansen, Philip Hallenborg, Anna-Kathrine Pedersen et al.
doi:10.1038/s41594-018-0084-y

Using UbiSite, an antibody-based approach that specifically detects protein lysine and N-terminal ubiquitination, Blagoev and colleagues uncover lack of correlation between changes in protein ubiquitination and abundance upon proteasome inhibition.

 

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