Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes.
Current challenges in the field of structural genomics point to the need for new tools and technologies for obtaining structures of macromolecular protein complexes. Here, we present an integrative computational method that uses molecular modelling, ion mobility-mass spectrometry (IM-MS) and incompl...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2010-08-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2919415?pdf=render |
| _version_ | 1818178212182622208 |
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| author | Argyris Politis Ah Young Park Suk-Joon Hyung Daniel Barsky Brandon T Ruotolo Carol V Robinson |
| author_facet | Argyris Politis Ah Young Park Suk-Joon Hyung Daniel Barsky Brandon T Ruotolo Carol V Robinson |
| author_sort | Argyris Politis |
| collection | DOAJ |
| description | Current challenges in the field of structural genomics point to the need for new tools and technologies for obtaining structures of macromolecular protein complexes. Here, we present an integrative computational method that uses molecular modelling, ion mobility-mass spectrometry (IM-MS) and incomplete atomic structures, usually from X-ray crystallography, to generate models of the subunit architecture of protein complexes. We begin by analyzing protein complexes using IM-MS, and by taking measurements of both intact complexes and sub-complexes that are generated in solution. We then examine available high resolution structural data and use a suite of computational methods to account for missing residues at the subunit and/or domain level. High-order complexes and sub-complexes are then constructed that conform to distance and connectivity constraints imposed by IM-MS data. We illustrate our method by applying it to multimeric protein complexes within the Escherichia coli replisome: the sliding clamp, (beta2), the gamma complex (gamma3deltadelta'), the DnaB helicase (DnaB6) and the Single-Stranded Binding Protein (SSB4). |
| first_indexed | 2024-12-11T20:44:23Z |
| format | Article |
| id | doaj.art-4c40f5c1ab26425f9f9a84179eb50141 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T20:44:23Z |
| publishDate | 2010-08-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-4c40f5c1ab26425f9f9a84179eb501412022-12-22T00:51:25ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-08-0158e1208010.1371/journal.pone.0012080Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes.Argyris PolitisAh Young ParkSuk-Joon HyungDaniel BarskyBrandon T RuotoloCarol V RobinsonCurrent challenges in the field of structural genomics point to the need for new tools and technologies for obtaining structures of macromolecular protein complexes. Here, we present an integrative computational method that uses molecular modelling, ion mobility-mass spectrometry (IM-MS) and incomplete atomic structures, usually from X-ray crystallography, to generate models of the subunit architecture of protein complexes. We begin by analyzing protein complexes using IM-MS, and by taking measurements of both intact complexes and sub-complexes that are generated in solution. We then examine available high resolution structural data and use a suite of computational methods to account for missing residues at the subunit and/or domain level. High-order complexes and sub-complexes are then constructed that conform to distance and connectivity constraints imposed by IM-MS data. We illustrate our method by applying it to multimeric protein complexes within the Escherichia coli replisome: the sliding clamp, (beta2), the gamma complex (gamma3deltadelta'), the DnaB helicase (DnaB6) and the Single-Stranded Binding Protein (SSB4).http://europepmc.org/articles/PMC2919415?pdf=render |
| spellingShingle | Argyris Politis Ah Young Park Suk-Joon Hyung Daniel Barsky Brandon T Ruotolo Carol V Robinson Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. PLoS ONE |
| title | Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. |
| title_full | Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. |
| title_fullStr | Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. |
| title_full_unstemmed | Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. |
| title_short | Integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes. |
| title_sort | integrating ion mobility mass spectrometry with molecular modelling to determine the architecture of multiprotein complexes |
| url | http://europepmc.org/articles/PMC2919415?pdf=render |
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