INVERTED TOPOLOGIES IN MEMBRANE PROTEINS: A MINI-REVIEW
Helical membrane proteins such as transporters, receptors, or channels often exhibit structural symmetry. Symmetry is perfect in homo-oligomers consisting of two or more copies of the same protein chain. Intriguingly, in single chain membrane proteins, often internal pseudo-symmetry is observed, in...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Elsevier
2013-08-01
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| Series: | Computational and Structural Biotechnology Journal |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2001037014600167 |
| _version_ | 1818505523121618944 |
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| author | Amanda M Duran Jens Meiler |
| author_facet | Amanda M Duran Jens Meiler |
| author_sort | Amanda M Duran |
| collection | DOAJ |
| description | Helical membrane proteins such as transporters, receptors, or channels often exhibit structural symmetry. Symmetry is perfect in homo-oligomers consisting of two or more copies of the same protein chain. Intriguingly, in single chain membrane proteins, often internal pseudo-symmetry is observed, in particular in transporters and channels. In several cases single chain proteins with pseudo-symmetry exist, that share the fold with homo-oligomers suggesting evolutionary pathways that involve gene duplication and fusion. It has been hypothesized that such evolutionary pathways allow for the rapid development of large proteins with novel functionality. At the same time symmetry can be leveraged to recognize highly symmetric substrates such as ions. Here we review helical transporter proteins with an inverted two-fold pseudo-symmetry. In this special scenario the symmetry axis lies in the membrane plane. As a result, the putative ancestral monomeric protein would insert in both directions into the membrane and its open-to-the-inside and open-to-the-outside conformations would be structurally identical and iso-energetic, giving a possible evolutionary pathway to create a transporter protein that needs to flip between the two states. |
| first_indexed | 2024-12-10T21:51:56Z |
| format | Article |
| id | doaj.art-804f089e91454c8ebb2084e58f7702a3 |
| institution | Directory Open Access Journal |
| issn | 2001-0370 |
| language | English |
| last_indexed | 2024-12-10T21:51:56Z |
| publishDate | 2013-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Computational and Structural Biotechnology Journal |
| spelling | doaj.art-804f089e91454c8ebb2084e58f7702a32022-12-22T01:32:10ZengElsevierComputational and Structural Biotechnology Journal2001-03702013-08-0181110.5936/csbj.201308004INVERTED TOPOLOGIES IN MEMBRANE PROTEINS: A MINI-REVIEWAmanda M Duran0Jens Meiler1Center for Structural Biology, Department of Chemistry, Vanderbilt University, Nashville, TN 37212, USACenter for Structural Biology, Department of Chemistry, Vanderbilt University, Nashville, TN 37212, USAHelical membrane proteins such as transporters, receptors, or channels often exhibit structural symmetry. Symmetry is perfect in homo-oligomers consisting of two or more copies of the same protein chain. Intriguingly, in single chain membrane proteins, often internal pseudo-symmetry is observed, in particular in transporters and channels. In several cases single chain proteins with pseudo-symmetry exist, that share the fold with homo-oligomers suggesting evolutionary pathways that involve gene duplication and fusion. It has been hypothesized that such evolutionary pathways allow for the rapid development of large proteins with novel functionality. At the same time symmetry can be leveraged to recognize highly symmetric substrates such as ions. Here we review helical transporter proteins with an inverted two-fold pseudo-symmetry. In this special scenario the symmetry axis lies in the membrane plane. As a result, the putative ancestral monomeric protein would insert in both directions into the membrane and its open-to-the-inside and open-to-the-outside conformations would be structurally identical and iso-energetic, giving a possible evolutionary pathway to create a transporter protein that needs to flip between the two states.http://www.sciencedirect.com/science/article/pii/S2001037014600167Membrane proteinsymmetryinverted topologygene duplicationgene fusionpseudo-symmetry |
| spellingShingle | Amanda M Duran Jens Meiler INVERTED TOPOLOGIES IN MEMBRANE PROTEINS: A MINI-REVIEW Computational and Structural Biotechnology Journal Membrane protein symmetry inverted topology gene duplication gene fusion pseudo-symmetry |
| title | INVERTED TOPOLOGIES IN MEMBRANE PROTEINS: A MINI-REVIEW |
| title_full | INVERTED TOPOLOGIES IN MEMBRANE PROTEINS: A MINI-REVIEW |
| title_fullStr | INVERTED TOPOLOGIES IN MEMBRANE PROTEINS: A MINI-REVIEW |
| title_full_unstemmed | INVERTED TOPOLOGIES IN MEMBRANE PROTEINS: A MINI-REVIEW |
| title_short | INVERTED TOPOLOGIES IN MEMBRANE PROTEINS: A MINI-REVIEW |
| title_sort | inverted topologies in membrane proteins a mini review |
| topic | Membrane protein symmetry inverted topology gene duplication gene fusion pseudo-symmetry |
| url | http://www.sciencedirect.com/science/article/pii/S2001037014600167 |
| work_keys_str_mv | AT amandamduran invertedtopologiesinmembraneproteinsaminireview AT jensmeiler invertedtopologiesinmembraneproteinsaminireview |