1e12

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(New page: 200px<br /> <applet load="1e12" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e12, resolution 1.8&Aring;" /> '''HALORHODOPSIN, A LIG...)
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<applet load="1e12" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1e12, resolution 1.8&Aring;" />
'''HALORHODOPSIN, A LIGHT-DRIVEN CHLORIDE PUMP'''<br />
'''HALORHODOPSIN, A LIGHT-DRIVEN CHLORIDE PUMP'''<br />
==Overview==
==Overview==
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Halorhodopsin, an archaeal rhodopsin ubiquitous in Haloarchaea, uses light, energy to pump chloride through biological membranes. Halorhodopsin, crystals were grown in a cubic lipidic phase, which allowed the x-ray, structure determination of this anion pump at 1.8 angstrom resolution., Halorhodopsin assembles to trimers around a central patch consisting of, palmitic acid. Next to the protonated Schiff base between Lys(242) and the, isomerizable retinal chromophore, a single chloride ion occupies the, transport site. Energetic calculations on chloride binding reveal a, combination of ion-ion and ion-dipole interactions for stabilizing the, anion 18 angstroms below the membrane surface. Ion dragging across the, protonated Schiff base explains why chloride and proton translocation, modes are mechanistically equivalent in archaeal rhodopsins.
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Halorhodopsin, an archaeal rhodopsin ubiquitous in Haloarchaea, uses light energy to pump chloride through biological membranes. Halorhodopsin crystals were grown in a cubic lipidic phase, which allowed the x-ray structure determination of this anion pump at 1.8 angstrom resolution. Halorhodopsin assembles to trimers around a central patch consisting of palmitic acid. Next to the protonated Schiff base between Lys(242) and the isomerizable retinal chromophore, a single chloride ion occupies the transport site. Energetic calculations on chloride binding reveal a combination of ion-ion and ion-dipole interactions for stabilizing the anion 18 angstroms below the membrane surface. Ion dragging across the protonated Schiff base explains why chloride and proton translocation modes are mechanistically equivalent in archaeal rhodopsins.
==About this Structure==
==About this Structure==
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1E12 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with CL, K, RET, PLM and MPG as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1E12 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb27_1.html Bacteriorhodopsin]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E12 OCA].
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1E12 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=RET:'>RET</scene>, <scene name='pdbligand=PLM:'>PLM</scene> and <scene name='pdbligand=MPG:'>MPG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1E12 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb27_1.html Bacteriorhodopsin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E12 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Besir, H.]]
[[Category: Besir, H.]]
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[[Category: Essen, L.O.]]
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[[Category: Essen, L O.]]
[[Category: Kolbe, M.]]
[[Category: Kolbe, M.]]
[[Category: Oesterhelt, D.]]
[[Category: Oesterhelt, D.]]
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[[Category: retinal protein]]
[[Category: retinal protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 08:59:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:38 2008''

Revision as of 10:22, 21 February 2008

Image:1e12.gif

1e12, resolution 1.8Å

Drag the structure with the mouse to rotate

HALORHODOPSIN, A LIGHT-DRIVEN CHLORIDE PUMP

Overview

Halorhodopsin, an archaeal rhodopsin ubiquitous in Haloarchaea, uses light energy to pump chloride through biological membranes. Halorhodopsin crystals were grown in a cubic lipidic phase, which allowed the x-ray structure determination of this anion pump at 1.8 angstrom resolution. Halorhodopsin assembles to trimers around a central patch consisting of palmitic acid. Next to the protonated Schiff base between Lys(242) and the isomerizable retinal chromophore, a single chloride ion occupies the transport site. Energetic calculations on chloride binding reveal a combination of ion-ion and ion-dipole interactions for stabilizing the anion 18 angstroms below the membrane surface. Ion dragging across the protonated Schiff base explains why chloride and proton translocation modes are mechanistically equivalent in archaeal rhodopsins.

About this Structure

1E12 is a Single protein structure of sequence from Halobacterium salinarum with , , , and as ligands. The following page contains interesting information on the relation of 1E12 with [Bacteriorhodopsin]. Full crystallographic information is available from OCA.

Reference

Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution., Kolbe M, Besir H, Essen LO, Oesterhelt D, Science. 2000 May 26;288(5470):1390-6. PMID:10827943

Page seeded by OCA on Thu Feb 21 12:22:38 2008

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