1m0l
From Proteopedia
(New page: 200px<br /><applet load="1m0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m0l, resolution 1.47Å" /> '''BACTERIORHODOPSIN/LI...) |
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| - | [[Image:1m0l.jpg|left|200px]]<br /><applet load="1m0l" size=" | + | [[Image:1m0l.jpg|left|200px]]<br /><applet load="1m0l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m0l, resolution 1.47Å" /> | caption="1m0l, resolution 1.47Å" /> | ||
'''BACTERIORHODOPSIN/LIPID COMPLEX AT 1.47 A RESOLUTION'''<br /> | '''BACTERIORHODOPSIN/LIPID COMPLEX AT 1.47 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The K state, an early intermediate of the bacteriorhodopsin photocycle, contains the excess free energy used for light-driven proton transport. | + | The K state, an early intermediate of the bacteriorhodopsin photocycle, contains the excess free energy used for light-driven proton transport. The energy gain must reside in or near the photoisomerized retinal, but in what form has long been an open question. We produced the K intermediate in bacteriorhodopsin crystals in a photostationary state at 100K, with 40% yield, and determined its X-ray diffraction structure to 1.43 A resolution. In independent refinements of data from four crystals, the changes are confined mainly to the photoisomerized retinal. The retinal is 13-cis,15-anti, as known from vibrational spectroscopy. The C13=C14 bond is rotated nearly fully to cis from the initial trans configuration, but the C14-C15 and C15=NZ bonds are partially counter-rotated. This strained geometry keeps the direction of the Schiff base N-H bond vector roughly in the extracellular direction, but the angle of its hydrogen bond with water 402, that connects it to the anionic Asp85 and Asp212, is not optimal. Weakening of this hydrogen bond may account for many of the reported features of the infrared spectrum of K, and for its photoelectric signal, as well as the deprotonation of the Schiff base later in the cycle. Importantly, although 13-cis, the retinal does not assume the expected bent shape of this configuration. Comparison of the calculated energy of the increased angle of C12-C13=C14, that allows this distortion, with the earlier reported calorimetric measurement of the enthalpy gain of the K state indicates that a significant part of the excess energy is conserved in the bond strain at C13. |
==About this Structure== | ==About this Structure== | ||
| - | 1M0L 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 LI1, SQU and RET as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1M0L 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=LI1:'>LI1</scene>, <scene name='pdbligand=SQU:'>SQU</scene> and <scene name='pdbligand=RET:'>RET</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M0L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lanyi, J | + | [[Category: Lanyi, J K.]] |
[[Category: LI1]] | [[Category: LI1]] | ||
[[Category: RET]] | [[Category: RET]] | ||
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[[Category: serpentine]] | [[Category: serpentine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:12 2008'' |
Revision as of 11:50, 21 February 2008
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BACTERIORHODOPSIN/LIPID COMPLEX AT 1.47 A RESOLUTION
Overview
The K state, an early intermediate of the bacteriorhodopsin photocycle, contains the excess free energy used for light-driven proton transport. The energy gain must reside in or near the photoisomerized retinal, but in what form has long been an open question. We produced the K intermediate in bacteriorhodopsin crystals in a photostationary state at 100K, with 40% yield, and determined its X-ray diffraction structure to 1.43 A resolution. In independent refinements of data from four crystals, the changes are confined mainly to the photoisomerized retinal. The retinal is 13-cis,15-anti, as known from vibrational spectroscopy. The C13=C14 bond is rotated nearly fully to cis from the initial trans configuration, but the C14-C15 and C15=NZ bonds are partially counter-rotated. This strained geometry keeps the direction of the Schiff base N-H bond vector roughly in the extracellular direction, but the angle of its hydrogen bond with water 402, that connects it to the anionic Asp85 and Asp212, is not optimal. Weakening of this hydrogen bond may account for many of the reported features of the infrared spectrum of K, and for its photoelectric signal, as well as the deprotonation of the Schiff base later in the cycle. Importantly, although 13-cis, the retinal does not assume the expected bent shape of this configuration. Comparison of the calculated energy of the increased angle of C12-C13=C14, that allows this distortion, with the earlier reported calorimetric measurement of the enthalpy gain of the K state indicates that a significant part of the excess energy is conserved in the bond strain at C13.
About this Structure
1M0L is a Single protein structure of sequence from Halobacterium salinarum with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal., Schobert B, Cupp-Vickery J, Hornak V, Smith S, Lanyi J, J Mol Biol. 2002 Aug 23;321(4):715-26. PMID:12206785
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