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Structural mechanis...
Structural mechanism of plant aquaporin gating
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- Tornroth-Horsefield, S (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Wang, Yi (författare)
- University of Illinois
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- Hedfalk, Kristina, 1969 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Johanson, Urban (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Karlsson, Maria (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Tajkhorshid, Emad (författare)
- University of Illinois
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- Neutze, Richard, 1969 (författare)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Kjellbom, Per (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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(creator_code:org_t)
- 2005-12-07
- 2006
- Engelska.
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Ingår i: Nature. - : Springer Science and Business Media LLC. - 0028-0836 .- 1476-4687. ; 439:7077, s. 688-694
- Relaterad länk:
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Abstract
Ämnesord
Stäng
- Plants counteract fluctuations in water supply by regulating all aquaporins in the cell plasma membrane. Channel closure results either from the dephosphorylation of two conserved serine residues under conditions of drought stress, or from the protonation of a conserved histidine residue following a drop in cytoplasmic pH due to anoxia during flooding. Here we report the X-ray structure of the spinach plasma membrane aquaporin SoPIP2; 1 in its closed conformation at 2.1 angstrom resolution and in its open conformation at 3.9 angstrom resolution, and molecular dynamics simulations of the initial events governing gating. In the closed conformation loop D caps the channel from the cytoplasm and thereby occludes the pore. In the open conformation loop D is displaced up to 16 angstrom and this movement opens a hydrophobic gate blocking the channel entrance from the cytoplasm. These results reveal a molecular gating mechanism which appears conserved throughout all plant plasma membrane aquaporins.
Ämnesord
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Nyckelord
- PERMEATION
- TRANSPORT
- PROTEIN
- ELECTRON-DENSITY MAPS
- MOLECULAR-MECHANISMS
- WATER CHANNEL
- PROTON EXCLUSION
- MEMBRANE AQUAPORIN
- GLYCEROL CONDUCTION
- DYNAMICS
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
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