1y8s: Difference between revisions
New page: '''Theoretical Model''' The entry 1Y8S is a Theoretical Model titled 'Theoretical model of the proton-proline symporter ProP'. Category:Theoretical Model ''Page seeded by [http://o... |
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{{Theoretical_model}} | |||
==THEORETICAL MODEL OF THE PROTON-PROLINE SYMPORTER PROP== | |||
<StructureSection load='1y8s' size='340' side='right'caption='[[1y8s]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y8S FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y8s FirstGlance], [https://www.ebi.ac.uk/pdbsum/1y8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y8s ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Transporter ProP of Escherichia coli, a member of the major facilitator superfamily (MFS), acts as an osmosensor and an osmoregulator in cells and after purification and reconstitution in proteoliposomes. H(+)-osmoprotectant symport via ProP is activated when medium osmolality is elevated with membrane impermeant osmolytes. The three-dimensional structure of ProP was modeled with the crystal structure of MFS member GlpT as a template. This GlpT structure represents the inward (or cytoplasm)-facing conformation predicted by the alternating access model for transport. LacZ-PhoA fusion analysis and site-directed fluorescence labeling substantiated the membrane topology and orientation predicted by this model and most hydropathy analyses. The model predicts the presence of a proton pathway within the N-terminal six-helix bundle of ProP (as opposed to the corresponding pathway found within the C-terminal helix bundle of its paralogue, LacY). Replacement of residues within the N-terminal helix bundle impaired the osmotic activation of ProP, providing the first indication that residues outside the C-terminal domain are involved in osmosensing. Some residues that were accessible from the periplasmic side, as predicted by the structural model, were more susceptible to covalent labeling in permeabilized membrane fractions than in intact bacteria. These residues may be accessible from the cytoplasmic side in structures not represented by our current model, or their limited exposure in vivo may reflect constraints on transporter structure that are related to its osmosensory mechanism. | |||
A structural model for the osmosensor, transporter, and osmoregulator ProP of Escherichia coli.,Wood JM, Culham DE, Hillar A, Vernikovska YI, Liu F, Boggs JM, Keates RA Biochemistry. 2005 Apr 19;44(15):5634-46. PMID:15823022<ref>PMID:15823022</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1y8s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Boggs, J M]] | |||
[[Category: Culham, D E]] | |||
[[Category: Hillar, A]] | |||
[[Category: Keates, R A]] | |||
[[Category: Liu, F]] | |||
[[Category: Vernikovska, Y I]] | |||
[[Category: Wood, J M]] | |||
Latest revision as of 19:24, 3 November 2021
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THEORETICAL MODEL OF THE PROTON-PROLINE SYMPORTER PROPTHEORETICAL MODEL OF THE PROTON-PROLINE SYMPORTER PROP
Structural highlights
Publication Abstract from PubMedTransporter ProP of Escherichia coli, a member of the major facilitator superfamily (MFS), acts as an osmosensor and an osmoregulator in cells and after purification and reconstitution in proteoliposomes. H(+)-osmoprotectant symport via ProP is activated when medium osmolality is elevated with membrane impermeant osmolytes. The three-dimensional structure of ProP was modeled with the crystal structure of MFS member GlpT as a template. This GlpT structure represents the inward (or cytoplasm)-facing conformation predicted by the alternating access model for transport. LacZ-PhoA fusion analysis and site-directed fluorescence labeling substantiated the membrane topology and orientation predicted by this model and most hydropathy analyses. The model predicts the presence of a proton pathway within the N-terminal six-helix bundle of ProP (as opposed to the corresponding pathway found within the C-terminal helix bundle of its paralogue, LacY). Replacement of residues within the N-terminal helix bundle impaired the osmotic activation of ProP, providing the first indication that residues outside the C-terminal domain are involved in osmosensing. Some residues that were accessible from the periplasmic side, as predicted by the structural model, were more susceptible to covalent labeling in permeabilized membrane fractions than in intact bacteria. These residues may be accessible from the cytoplasmic side in structures not represented by our current model, or their limited exposure in vivo may reflect constraints on transporter structure that are related to its osmosensory mechanism. A structural model for the osmosensor, transporter, and osmoregulator ProP of Escherichia coli.,Wood JM, Culham DE, Hillar A, Vernikovska YI, Liu F, Boggs JM, Keates RA Biochemistry. 2005 Apr 19;44(15):5634-46. PMID:15823022[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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