Conservation of conformational dynamics across prokaryotic actins

The actin family of cytoskeletal proteins is essential to the physiology of virtually all archaea, bacteria, and eukaryotes. While X-ray crystallography and electron microscopy have revealed structural homologies among actin-family proteins, these techniques cannot probe molecular-scale conformation...

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Vydané v:	PLoS computational biology Ročník 15; číslo 4; s. e1006683
Hlavní autori:	Ng, Natalie, Shi, Handuo, Colavin, Alexandre, Huang, Kerwyn Casey
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States Public Library of Science 01.04.2019 Public Library of Science (PLoS)
Predmet:	Actin Actins - chemistry Archaea Bacteria Bacterial Proteins - chemistry Bioengineering Biology and Life Sciences Biophysics Cell division Computational Biology Crystallography Crystallography, X-Ray Cytoskeletal proteins Cytoskeletal Proteins - chemistry Cytoskeleton Dihedral angle Dimers E coli Electron microscopy Escherichia coli Proteins - chemistry Eukaryotes Family relations Funding Homology Microscopy Models, Molecular Molecular dynamics Molecular Dynamics Simulation Molecular structure Monomers Morphogenesis Muscle proteins Mutation Nucleotides Physical Sciences Physiological aspects Polymerization Prokaryotes Protein Conformation Protein Interaction Domains and Motifs Proteins Pyrobaculum - chemistry Rigid structures Software Structural Homology, Protein Supervision X-ray crystallography United States > US
ISSN:	1553-7358, 1553-734X, 1553-7358
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