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The DARC site: a database of aligned ribosomal complexes

The ribosome is a highly dynamic machine responsible for protein synthesis within the cell. Cryo-electron microscopy (cryo-EM) and X-ray crystallography structures of ribosomal particles, alone and in complex with diverse ligands (protein factors, RNAs and small molecules), have revealed the dynamic...

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Autores principales: Jarasch, Alexander, Dziuk, Philipp, Becker, Thomas, Armache, Jean-Paul, Hauser, Andreas, Wilson, Daniel N., Beckmann, Roland
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245104/
https://www.ncbi.nlm.nih.gov/pubmed/22009674
http://dx.doi.org/10.1093/nar/gkr824
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author Jarasch, Alexander
Dziuk, Philipp
Becker, Thomas
Armache, Jean-Paul
Hauser, Andreas
Wilson, Daniel N.
Beckmann, Roland
author_facet Jarasch, Alexander
Dziuk, Philipp
Becker, Thomas
Armache, Jean-Paul
Hauser, Andreas
Wilson, Daniel N.
Beckmann, Roland
author_sort Jarasch, Alexander
collection PubMed
description The ribosome is a highly dynamic machine responsible for protein synthesis within the cell. Cryo-electron microscopy (cryo-EM) and X-ray crystallography structures of ribosomal particles, alone and in complex with diverse ligands (protein factors, RNAs and small molecules), have revealed the dynamic nature of the ribosome and provided much needed insight into translation and its regulation. In the past years, there has been exponential growth in the deposition of cryo-EM maps into the Electron Microscopy Data Bank (EMDB) as well as atomic structures into the Protein Data Bank (PDB). Unfortunately, the deposited ribosomal particles usually have distinct orientations with respect to one another, which complicate the comparison of the available structures. To simplify this, we have developed a Database of Aligned Ribosomal Complexes, the DARC site (http://darcsite.genzentrum.lmu.de/darc/), which houses the available cryo-EM maps and atomic coordinates of ribosomal particles from the EMDB and PDB aligned within a common coordinate system. An easy-to-use, searchable interface allows users to access and download >130 cryo-EM maps and >300 atomic models in the format of brix and pdb files, respectively. The aligned coordinate system substantially simplifies direct visualization of conformational changes in the ribosome, such as subunit rotation and head-swiveling, as well as direct comparison of bound ligands, such as antibiotics or translation factors.
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spelling pubmed-32451042012-01-10 The DARC site: a database of aligned ribosomal complexes Jarasch, Alexander Dziuk, Philipp Becker, Thomas Armache, Jean-Paul Hauser, Andreas Wilson, Daniel N. Beckmann, Roland Nucleic Acids Res Articles The ribosome is a highly dynamic machine responsible for protein synthesis within the cell. Cryo-electron microscopy (cryo-EM) and X-ray crystallography structures of ribosomal particles, alone and in complex with diverse ligands (protein factors, RNAs and small molecules), have revealed the dynamic nature of the ribosome and provided much needed insight into translation and its regulation. In the past years, there has been exponential growth in the deposition of cryo-EM maps into the Electron Microscopy Data Bank (EMDB) as well as atomic structures into the Protein Data Bank (PDB). Unfortunately, the deposited ribosomal particles usually have distinct orientations with respect to one another, which complicate the comparison of the available structures. To simplify this, we have developed a Database of Aligned Ribosomal Complexes, the DARC site (http://darcsite.genzentrum.lmu.de/darc/), which houses the available cryo-EM maps and atomic coordinates of ribosomal particles from the EMDB and PDB aligned within a common coordinate system. An easy-to-use, searchable interface allows users to access and download >130 cryo-EM maps and >300 atomic models in the format of brix and pdb files, respectively. The aligned coordinate system substantially simplifies direct visualization of conformational changes in the ribosome, such as subunit rotation and head-swiveling, as well as direct comparison of bound ligands, such as antibiotics or translation factors. Oxford University Press 2012-01 2011-10-18 /pmc/articles/PMC3245104/ /pubmed/22009674 http://dx.doi.org/10.1093/nar/gkr824 Text en © The Author(s) 2011. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Articles
Jarasch, Alexander
Dziuk, Philipp
Becker, Thomas
Armache, Jean-Paul
Hauser, Andreas
Wilson, Daniel N.
Beckmann, Roland
The DARC site: a database of aligned ribosomal complexes
title The DARC site: a database of aligned ribosomal complexes
title_full The DARC site: a database of aligned ribosomal complexes
title_fullStr The DARC site: a database of aligned ribosomal complexes
title_full_unstemmed The DARC site: a database of aligned ribosomal complexes
title_short The DARC site: a database of aligned ribosomal complexes
title_sort darc site: a database of aligned ribosomal complexes
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3245104/
https://www.ncbi.nlm.nih.gov/pubmed/22009674
http://dx.doi.org/10.1093/nar/gkr824
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