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Article: Population shift between the open and closed states changes the water permeability of an aquaporin Z mutant

TitlePopulation shift between the open and closed states changes the water permeability of an aquaporin Z mutant
Authors
Issue Date2012
PublisherCell Press. The Journal's web site is located at http://www.cell.com/biophysj/
Citation
Biophysical Journal, 2012, v. 103 n. 2, p. 212-218 How to Cite?
AbstractAquaporins are tetrameric transmembrane channels permeable to water and other small solutes. Wild-type (WT) and mutant Aquaporin Z (AqpZ) have been widely studied and multiple factors have been found to affect their water permeability. In this study, molecular dynamics simulations have been performed for the tetrameric AqpZ F43W/H174G/T183F mutant. It displayed ∼10% average water permeability compared to WT AqpZ, which had been attributed to the increased channel lumen hydrophobicity. Our simulations, however, show a ring stacking between W43 and F183 acting as a secondary steric gate in the triple mutant with R189 as the primary steric gate in both mutant and WT AqpZ. The double gates (R189 and W43-F183) result in a high population of the closed conformation in the mutant. Occasionally an open state, with diffusive water permeability very close to that of WT AqpZ, was observed. Taken together, our results show that the double-gate mechanism is sufficient to explain the reduced water permeability in the mutant without invoking effects arising from increased hydrophobicity of the channel lumen. Our findings provide insights into how aquaporin-mediated water transport can be modulated and may further point to how aquaporin function can be optimized for biomimetic membrane applications. © 2012 by the Biophysical Society.
Persistent Identifierhttp://hdl.handle.net/10722/185428
ISSN
2015 Impact Factor: 3.632
2015 SCImago Journal Rankings: 2.188
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorXin, Len_US
dc.contributor.authorHélixNielsen, Cen_US
dc.contributor.authorSu, Hen_US
dc.contributor.authorTorres, Jen_US
dc.contributor.authorTang, Cen_US
dc.contributor.authorWang, Ren_US
dc.contributor.authorFane, AGen_US
dc.contributor.authorMu, Yen_US
dc.date.accessioned2013-07-30T07:32:27Z-
dc.date.available2013-07-30T07:32:27Z-
dc.date.issued2012en_US
dc.identifier.citationBiophysical Journal, 2012, v. 103 n. 2, p. 212-218en_US
dc.identifier.issn0006-3495en_US
dc.identifier.urihttp://hdl.handle.net/10722/185428-
dc.description.abstractAquaporins are tetrameric transmembrane channels permeable to water and other small solutes. Wild-type (WT) and mutant Aquaporin Z (AqpZ) have been widely studied and multiple factors have been found to affect their water permeability. In this study, molecular dynamics simulations have been performed for the tetrameric AqpZ F43W/H174G/T183F mutant. It displayed ∼10% average water permeability compared to WT AqpZ, which had been attributed to the increased channel lumen hydrophobicity. Our simulations, however, show a ring stacking between W43 and F183 acting as a secondary steric gate in the triple mutant with R189 as the primary steric gate in both mutant and WT AqpZ. The double gates (R189 and W43-F183) result in a high population of the closed conformation in the mutant. Occasionally an open state, with diffusive water permeability very close to that of WT AqpZ, was observed. Taken together, our results show that the double-gate mechanism is sufficient to explain the reduced water permeability in the mutant without invoking effects arising from increased hydrophobicity of the channel lumen. Our findings provide insights into how aquaporin-mediated water transport can be modulated and may further point to how aquaporin function can be optimized for biomimetic membrane applications. © 2012 by the Biophysical Society.en_US
dc.languageengen_US
dc.publisherCell Press. The Journal's web site is located at http://www.cell.com/biophysj/en_US
dc.relation.ispartofBiophysical Journalen_US
dc.subject.meshAquaporins - Chemistry - Metabolismen_US
dc.subject.meshBiological Transporten_US
dc.subject.meshCell Membrane Permeabilityen_US
dc.subject.meshHydrogen Bondingen_US
dc.subject.meshIon Channel Gatingen_US
dc.subject.meshMolecular Dynamics Simulationen_US
dc.subject.meshMutant Proteins - Chemistry - Metabolismen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshWater - Metabolismen_US
dc.titlePopulation shift between the open and closed states changes the water permeability of an aquaporin Z mutanten_US
dc.typeArticleen_US
dc.identifier.emailTang, C: tangc@hku.hken_US
dc.identifier.authorityTang, C=rp01765en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.bpj.2012.05.049en_US
dc.identifier.pmid22853898-
dc.identifier.scopuseid_2-s2.0-84864762831en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84864762831&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume103en_US
dc.identifier.issue2en_US
dc.identifier.spage212en_US
dc.identifier.epage218en_US
dc.identifier.isiWOS:000306522300008-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridXin, L=35075384700en_US
dc.identifier.scopusauthoridHélixNielsen, C=36767484600en_US
dc.identifier.scopusauthoridSu, H=55224470200en_US
dc.identifier.scopusauthoridTorres, J=55323863800en_US
dc.identifier.scopusauthoridTang, C=35489259800en_US
dc.identifier.scopusauthoridWang, R=7405339682en_US
dc.identifier.scopusauthoridFane, AG=55132709000en_US
dc.identifier.scopusauthoridMu, Y=7103374032en_US

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