Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S

Chao Xu, Gaofeng Cui, Maria Victoria Botuyan, and Georges Mer
Structure
10.1016/j.str.2008.08.008
[Summary] [Full Text] [PDF] [Supplemental Data]

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Structural Analysis of the Interactions between Paxillin LD motifs and α-Parvin Sonja Lorenz, Ioannis Vakonakis, Edward D. Lowe, Iain D. Campbell, Martin E. M. Noble, and Maria K. Hoellerer [Summary] [Full Text] [PDF] [Supplemental Data]

Cell migration is a key process in embryonic morphogenesis, tissue repair, and the inflammatory response. The protein paxillin is known to be essential for cell migration through the formation of dynamic signaling complexes via five leucine rich regions, called “LD-motifs”. Study of the interaction between LD-motifs and the C-terminal calponin-homology domain of α-parvin, done by Lorenz et al., reveals that all five motifs can bind to a common binding site on α-parvin, apparently in either of two antiparallel orientations. It is speculated that this surprising degree of promiscuity evolved to mediate the formation of multi-protein complexes in vivo.

In This Issue

	In Review: Crystallography with DARPins The structure of proteins which are difficult to crystallize can often be solved by forming a non-covalent complex with a helper protein – a crystallization “chaperone”. A valuable addition to the present repertoire of crystallization “chaperones” is the recently developed Designed Ankyrin Repeat Protein (DARPin) technology. Sennhauser et al. now review this technology and discuss its use in structural biology.
	Calmodulin-CaV2 IQ Domain Interplay Calmodulin plays a key role in voltage gated calcium channel, CaV, modulation. Specific Ca2+/calmodulin lobes govern CaV inactivation and facilitation through interactions with the pore-forming subunit IQ domain. Kim et al. analyze the origins of calmodulin-CaV2 IQ domain interactions and find binding orientations opposite to those previously described for CaV1 IQ domain-calmodulin complexes, unveiling the remarkable structural plasticity underlying CaV feedback modulation.
	Rab27 Gone Fishing! Rab27A is required for actin-based melanosome transport in mammalian skin melanocytes and peripheral localization of melanosome and glucagon granules, through its interaction with specific effectors, Slac2-a/melanophilin and Exophilin4/Slp2-a. Chavas et al. describe the structure of Rab27A/Exophilin4 RBD27 complex and Kukimoto-Niino et al. describe the structure of the constitutively-active form of Rab27B complexed with GTP and the effector domain of Slac2-a. (Figure credits: Chavas et al.)
	Story of Two Rings Pontin and reptin are essential for the assembly of several chromatin remodeling and ribonucleoprotein complexes, including telomerase. Torreira et al. propose a structural model of the yeast pontin/reptin complex based on a cryo-electron microscopy reconstruction of in vivo assembled complexes. Each protein forms one hexameric ring and two rings interact using flexible domains projecting from each hexamer. (Figure adopted from: Torreira et al.)
	Behold the Seneca Valley Virus Venkataraman et al. describe the crystal structure of Seneca Valley Virus-001 (SVV-001), the representative member of a new genus “Senecavirus” in the family Picornaviridae. SVV-001 is the first naturally occurring non-pathogenic picornavirus shown to mediate selective cytotoxicity towards tumor cells with neuroendocrine cancer features. (Figure credits: Venkataraman et al.)

In Review

PACemakers of Proteasome Core Particle Assembly

Paula C. Ramos and R. Jürgen Dohmen

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Structure 16(9), 1296

Protein-Protein Interactions in the Membrane: Sequence, Structural, and Biological Motifs
David T. Moore, Bryan W. Berger, and William F. DeGrado
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Structure 16(7), 991

The Mechanics of Translocation: A Molecular “Spring-and-Ratchet” System
Stephen J. Moran, John F. Flanagan, Olivier Namy, David I. Stuart, Ian Brierley, and Robert J.C. Gilbert
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Structure 16(5), 664

Mammalian DNA Methyltransferases: A Structural Perspective
Xiaodong Cheng and Robert M. Blumenthal
[Summary] [Full Text] [PDF]
Structure 16(3), 341

H2A.Z: View from the Top
Jordanka Zlatanova and Amit Thakar
[Summary] [Full Text] [PDF] [Supplemental Data]
Structure 16(2), 166

The following are recently described tools for structural biologists

Accurate NMR Structures Through Minimization of an Extended Hybrid Energy

Michael Nilges, Aymeric Bernard, Benjamin Bardiaux, Thérèse Malliavin, Michael Habeck and Wolfgang Rieping

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Structure 16(9), 1305

A Lipidic-Sponge Phase Screen for Membrane Protein Crystallization
Annemarie B. Wöhri, Linda C. Johansson, Pia Wadsten-Hindrichsen, Weixiao Y. Wahlgren, Gerhard Fischer, Rob Horsefield, Gergely Katona, Maria Nyblom, Fredrik Öberg, Gillian Young, Richard J. Cogdell, Niall J. Fraser, Sven Engström, and Richard Neutze
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Structure 16(7), 1003

Preparation of Multimilligram Quantities of Large, Linear DNA Molecules for Structural Studies
Merlind Muecke, Martin Samuels, Megan Davey, and David Jeruzalmi
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Structure 16(6), 837

Flexible Fitting of Atomic Structures into Electron Microscopy Maps Using Molecular Dynamics
Leonardo G. Trabuco, Elizabeth Villa, Kakoli Mitra, Joachim Frank, and Klaus Schulten
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Structure 16(5), 673

Microscale Fluorescent Thermal Stability Assay for Membrane Proteins
Alexander I. Alexandrov, Mauro Mileni, Ellen Y.T. Chien, Michael A. Hanson, and Raymond C. Stevens
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Structure 16 (3), 351

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