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Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility.
PilT is a hexameric ATPase required for bacterial type IV pilus retraction and surface motility. Crystal structures of ADP- and ATP-bound Aquifex aeolicus PilT at 2.8 and 3.2 A resolution showExpand
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Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution.
The structure of troponin C has been refined at 2A resolution to an R value of 0.172 using a total of 8,100 reflections. Troponin C has an unusual dumbbell shape with only the two C-domain highExpand
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Structure-guided Engineering Enhances a Phytochrome-based Infrared Fluorescent Protein*
Background: Engineered variants of the phytochrome photoreceptor are infrared fluorescent proteins. Results: Based on crystal structures, side chain substitutions near the chromophore were combinedExpand
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The structural basis for tight control of PP2A methylation and function by LCMT-1.
Proper formation of protein phosphatase 2A (PP2A) holoenzymes is essential for the fitness of all eukaryotic cells. Carboxyl methylation of the PP2A catalytic subunit plays a critical role inExpand
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Site-Directed Spin Labeling Reveals Pentameric Ligand-Gated Ion Channel Gating Motions
Pentameric ligand-gated ion channels (pLGICs) are neurotransmitter-activated receptors that mediate fast synaptic transmission. In pLGICs, binding of agonist to the extracellular domain triggers aExpand
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Structural requirements for eszopiclone and zolpidem binding to the gamma-aminobutyric acid type-A (GABAA) receptor are different.
The sleep-aids zolpidem and eszopiclone exert their effects by binding to and modulating gamma-aminobutyric acid type-A receptors (GABA(A)Rs), but little is known about the structural requirementsExpand
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Molecular mechanism and evolution of guanylate kinase regulation by (p)ppGpp.
The nucleotide (p)ppGpp mediates bacterial stress responses, but its targets and underlying mechanisms of action vary among bacterial species and remain incompletely understood. Here, we characterizeExpand
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Catalytic activation of histone acetyltransferase Rtt109 by a histone chaperone
Most histone acetyltransferases (HATs) function as multisubunit complexes in which accessory proteins regulate substrate specificity and catalytic efficiency. Rtt109 is a particularly interestingExpand
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Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation
The B″/PR72 family of protein phosphatase 2A (PP2A) is an important PP2A family involved in diverse cellular processes, and uniquely regulated by calcium binding to the regulatory subunit. The PR70Expand
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Structural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone
Proper activation of protein phosphatase 2A (PP2A) catalytic subunit is central for the complex PP2A regulation and is crucial for broad aspects of cellular function. The crystal structure of PP2AExpand
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