Topic
Structural biology
About: Structural biology is a research topic. Over the lifetime, 2206 publications have been published within this topic receiving 126070 citations.
Papers published on a yearly basis
Papers
More filters
01 Jan 2016
TL;DR: The book includes thorough discussions on cytochrome oxidase including the use of the new non-destructive femtosecond diffraction before destruction X-ray free electron laser for diffraction analysis, and major sections on signaling, super-complexes, state transitions, and the interaction of linear and cyclic electron transport chains.
Abstract: Why study cytochrome complexes? An answer is in the subtitle of the book Evolution, Structures, Energy Transduction, and Signaling . Studies on the cytochrome family of proteins include and, influence, a wide range of theoretical and computational approaches, as well as a broad cross-section of experimental techniques. Studies of cytochromes and cytochrome complexes thus utilize an extraordinary range of experimental approaches, described in this volume, which include: computational biology, genetics, macromolecular biochemistry, molecular biology, the physics of charge transfer, structure analysis using x-ray and electron diffraction, and ultra-fast spectroscopy. This information and understanding exerts an influence on a wide spectrum of subjects in modern biology, including molecular evolution, mechanisms of membrane-based respiratory and photosynthetic energy transduction, theory of charge transfer in proteins, structure-function of large hetero-oligomeric membrane proteins, including lipid-protein interactions, and trans-membrane signaling. The book starts with a historical introduction that focuses on research in the first half of the 20th century, and the pre-World War II development in England of the field and its notation, proceeding to a discussion of the evolution of cytochromes and hemes, fundamentals of the theory of electron transfer in proteins, and an extensive description of molecular structures of cytochromes and of the cytochrome complexes. The latter information has had a major impact on the broad field of the structure-function of integral membrane proteins, the newest area of macromolecular structural biology. The book includes thorough discussions on cytochrome oxidase including the use of the new non-destructive femtosecond diffraction before destruction X-ray free electron laser for diffraction analysis, and major sections on signaling, super-complexes, state transitions, and the interaction of linear and cyclic electron transport chains. The extent of fundamental research areas included in this book makes it an important resource for the teaching of broad aspects of biological energy transduction to advanced undergraduate and graduate students with interests in biology, biochemistry, biological engineering, chemistry, and biophysics
33 citations
TL;DR: The data suggest that the essential Okp1 subunit is a multi‐segmented nexus with distinct binding sites for Ame1, Nkp1‐Nkp2 and Ctf19‐Mcm21, and that absence of this motif results in dependence on the mitotic checkpoint for viability.
Abstract: Kinetochores are dynamic cellular structures that connect chromosomes to microtubules. They form from multi‐protein assemblies that are evolutionarily conserved between yeasts and humans. One of these assemblies—COMA—consists of subunits Ame1 CENP‐U , Ctf19 CENP‐P , Mcm21 CENP‐O and Okp1 CENP‐Q . A description of COMA molecular organization has so far been missing. We defined the subunit topology of COMA, bound with inner kinetochore proteins Nkp1 and Nkp2, from the yeast Kluyveromyces lactis , with nanoflow electrospray ionization mass spectrometry, and mapped intermolecular contacts with hydrogen‐deuterium exchange coupled to mass spectrometry. Our data suggest that the essential Okp1 subunit is a multi‐segmented nexus with distinct binding sites for Ame1, Nkp1‐Nkp2 and Ctf19‐Mcm21. Our crystal structure of the Ctf19‐Mcm21 RWD domains bound with Okp1 shows the molecular contacts of this important inner kinetochore joint. The Ctf19‐Mcm21 binding motif in Okp1 configures a branch of mitotic inner kinetochores, by tethering Ctf19‐Mcm21 and Chl4 CENP‐N ‐Iml3 CENP‐L . Absence of this motif results in dependence on the mitotic checkpoint for viability.
33 citations
TL;DR: A molecular dynamics study of the Mlc1p-IQ2 protein-peptide complex is reported, starting with its crystal structure, and its dynamics in an aqueous solution, and the structure of the light-chain-binding domain of myosin V from the yeast S. cerevisiae is discussed.
33 citations
TL;DR: Molecular and structural biology of phosphorylated and glycosylated proteins expressed in eukaryotic expression systems which are especially suited for large-scale production of these proteins are reviewed.
32 citations
TL;DR: The cryo-EM structure of the XaxAB pore complex from Xenorhabdus nematophila and the crystal structures of the soluble monomers reveal that XaxA and XaxB are built similarly and appear as heterodimers in the 12–15 subunits containing pore, classifyingXaxAB as bi-component α-PFT.
Abstract: α-Xenorhabdolysins (Xax) are α-pore-forming toxins (α-PFT) that form 1-1.3 MDa large pore complexes to perforate the host cell membrane. PFTs are used by a variety of bacterial pathogens to attack host cells. Due to the lack of structural information, the molecular mechanism of action of Xax toxins is poorly understood. Here, we report the cryo-EM structure of the XaxAB pore complex from Xenorhabdus nematophila and the crystal structures of the soluble monomers of XaxA and XaxB. The structures reveal that XaxA and XaxB are built similarly and appear as heterodimers in the 12-15 subunits containing pore, classifying XaxAB as bi-component α-PFT. Major conformational changes in XaxB, including the swinging out of an amphipathic helix are responsible for membrane insertion. XaxA acts as an activator and stabilizer for XaxB that forms the actual transmembrane pore. Based on our results, we propose a novel structural model for the mechanism of Xax intoxication.
32 citations