Wednesday, June 6, 2018

Nature Structural & Molecular Biology Contents: 2018 Volume #25 pp 435 - 545

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June 2018 Volume 25, Issue 6

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Let K-Ras activate its own inhibitor    pp435 - 437
Alexander V. Statsyuk

Strength in numbers—an arrestin interaction code    pp437 - 439
Christopher J. Draper-Joyce & Arthur Christopoulos

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RBR ligase–mediated ubiquitin transfer: a tale with many twists and turns    pp440 - 445
Helen Walden & Katrin Rittinger

Rittinger and Walden review recent structural and functional insights to contrast and compare RBR E3 ubiquitin ligases and their regulation through autoinhibition, post-translational modifications, multimerization and protein-protein interactions.


Review Articles


RPA and RAD51: fork reversal, fork protection, and genome stability    pp446 - 453
Kamakoti P. Bhat & David Cortez

Bhat and Cortez discuss current knowledge on the multiple mechanisms by which RPA and RAD51 contribute to genome stability during DNA replication, in particular for replication fork reversal and fork protection.




The reactivity-driven biochemical mechanism of covalent KRASG12C inhibitors    pp454 - 462
Rasmus Hansen, Ulf Peters, Anjali Babbar, Yuching Chen, Jun Feng et al.

Kinetic and structural analyses show that the activity of two covalent inhibitors of human KRASG12C, which initially bind to a shallow pocket with low affinity, is driven by KRAS-mediated catalysis of the chemical reaction with Cys12.


Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation    pp463 - 471
Elizabeth L. Guenther, Qin Cao, Hamilton Trinh, Jiahui Lu, Michael R. Sawaya et al.

Segments from TDP-43 LCD form irreversible steric zippers typical of amyloid fibrils and labile interactions found in reversible assemblies. Familial ALS mutations or a phosphorylation event can convert reversible to irreversible aggregates.


Orthosteric and allosteric action of the C5a receptor antagonists    pp472 - 481
Heng Liu, Hee Ryung Kim, R. N. V. Krishna Deepak, Lei Wang, Ka Young Chung et al.

Structures of human C5aR in ternary complexes with the peptide antagonist PMX53 and a non-peptide antagonist, either avacopan or NDT9513727, reveal the orthosteric effects of PMX53, the allosteric effects of the non-peptide drugs and structural details of signal transduction by C5aR.


Dissection of DNA double-strand-break repair using novel single-molecule forceps    pp482 - 487
Jing L. Wang, Camille Duboc, Qian Wu, Takashi Ochi, Shikang Liang et al.

Single-molecule analyses using a DNA substrate with a bridge linker reveals a role of PAXX in molecular bridging of double-strand breaks to facilitate NHEJ-mediated repair.


Structural basis for signal recognition and transduction by platelet-activating-factor receptor    pp488 - 495
Can Cao, Qiuxiang Tan, Chanjuan Xu, Lingli He, Linlin Yang et al.

Crystal structures of PAFR in complex with the antagonist SR 27417 and the inverse agonist ABT-491, together with accompanying experiments, provide insight into recognition of PAF and reveal an unusual ligand-dependent conformation of helical bundle.


Distinct roles of cohesin-SA1 and cohesin-SA2 in 3D chromosome organization    pp496 - 504
Aleksandar Kojic, Ana Cuadrado, Magali De Koninck, Daniel Giménez-Llorente, Miriam Rodríguez-Corsino et al.

Depletion, ChIP and Hi-C analyses of the genomic distribution of the two variant cohesin complexes in human cells reveal non-redundant functions and differential contributions to 3D genome organization.


Controlling load-dependent kinetics of β-cardiac myosin at the single-molecule level    pp505 - 514
Chao Liu, Masataka Kawana, Dan Song, Kathleen M. Ruppel & James A. Spudich

The load-dependence of the detachment rate of single molecules of human β-cardiac myosin from actin, and the effects of small-molecule compounds and cardiomyopathy-causing mutations, are investigated using harmonic force spectroscopy.


Cryo-EM structure of the human neutral amino acid transporter ASCT2    pp515 - 521
Alisa A. Garaeva, Gert T. Oostergetel, Cornelius Gati, Albert Guskov, Cristina Paulino et al.

A cryo-EM structure of the human SLC1 transporter ASCT2 in the inward-facing conformation reveals the retrovirus-docking site and helps to elucidate the transport cycle. The transport domain is more solvent exposed than in most of the homolog structures.


Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state    pp522 - 527
Hsiang-Ting Lei, Jinming Ma, Silvia Sanchez Martinez & Tamir Gonen

The crystal structure of SLC38A9 from Danio rerio in complex with arginine in the cytosol-open conformation reveals the mechanism of substrate binding.


Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM    pp528 - 537
Felipe Merino, Sabrina Pospich, Johanna Funk, Thorsten Wagner, Florian Küllmer et al.

Cryo-EM structures of F-actin captured in different nucleotide states, by using nucleotide analogs or small molecules, reveal different conformational states linked to ATP hydrolysis.




Molecular mechanism of modulating arrestin conformation by GPCR phosphorylation    pp538 - 545
Andrija Sente, Raphael Peer, Ashish Srivastava, Mithu Baidya, Arthur M. Lesk et al.

Analysis of 18 available structures and other data reveals a new, conserved structural motif in arrestins and suggests that different phosphorylation patterns of the GPCR C terminus can drive distinct arrestin conformations and functional outcomes.


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