Cameron Mura
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The Mura lab employs experimental and computational approaches to understand the structure, function/dynamics, and evolution of RNA- and DNA-based protein assemblies. In particular, we seek a deeper understanding of ribonucleoprotein (RNP) assemblies – What these protein/RNA complexes look like at atomic resolution (structure), their assembly pathways and dynamical behavior (function), and the interrelationships between Sm and Sm-like systems (evolution).
Discovered as the antigens in the autoimmune disease lupus, Sm proteins are now known to form a broad, evolutionarily-conserved family that play key roles in most aspects of RNA metabolism (including mRNA splicing), as well as in bacterial cell-cell communication networks ("quorum sensing"). Sm-based complexes such as the spliceosome exceed the ribosome in terms of both size and architectural complexity, thereby providing an immensely rich area for ongoing studies. Current work focuses on Sm systems drawn from both a well-established context (splicing) and a more recently emerging area (quorum sensing) that is of major biomedical significance because of its involvement in biofilm-mediated bacterial pathogenesis. The research program being developed to pursue this work is necessarily highly interdisciplinary, relying particularly heavily on methods from structural biology (e.g., crystallography) and computational chemistry (e.g., molecular dynamics simulations), in addition to traditional wet-lab biochemistry.
(PDF icons link to local copies; DOI links to publishers; author names link to their webpages)
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Oxyanion-Mediated Inhibition of Serine Proteases
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The Crystal Structure of a Heptameric Archaeal Sm Protein:
Implications for the Sm Core of Eukaryotic SnRNPs
Popular scientific coverage:
Science Magazine "Editors' Choice" (18 May 2001) – Molecular Biology: At the Core of Splicing
Cover of Fall 2001 ACA Newsletter (upper left) -
Structure of a Nudix Protein from Pyrobaculum aerophilum Reveals a Dimer with Two
Intersubunit β-Sheets
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Structure and Function of an Archaeal Homolog of Survival Protein E (SurEα):
An Acid Phosphatase with Purine Nucleotide Specificity
(Supplementary Materials [PDF];
Erratum [HTML,
PDF])
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The Oligomerization and Ligand-binding Properties of Sm-like Archaeal Proteins (SmAPs)
Popular scientific coverage:
Cover Illustration
2003 PDB Holiday Postcard
2003 PDB Annual Report (see last page)
Cover Illustration of "Protein Crystallography" book by Lattman & Loll (2008)
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Structure and Assembly of an Augmented Sm-like Archaeal Protein 14-mer
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Three-dimensional Structures of Fibrillar Sm Proteins: Hfq and Other Sm-like Proteins
(Supplementary Materials [PDF])
Popular scientific coverage:
2006 San Diego Supercomputer Center (SDSC) Wall Calendar
2004 PDB Holiday Postcard (not from my work, but same Sm-like protein that was part of this study)
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Sm-like Protein Hfq: Location of the ATP-binding Site and the Effect of ATP on Hfq•RNA Complexes
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Molecular Dynamics of a κB DNA Element: Base Flipping via
Cross-strand Intercalative Stacking in a Microsecond-scale Simulation
∗: Corresponding authors
© 2008 University of Virginia Department of Chemistry

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