1qov

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(New page: 200px<br /><applet load="1qov" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qov, resolution 2.1&Aring;" /> '''PHOTOSYNTHETIC REACTI...)
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[[Image:1qov.gif|left|200px]]<br /><applet load="1qov" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qov.gif|left|200px]]<br /><applet load="1qov" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qov, resolution 2.1&Aring;" />
caption="1qov, resolution 2.1&Aring;" />
'''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M260 REPLACED WITH TRP (CHAIN M, A260W)'''<br />
'''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M260 REPLACED WITH TRP (CHAIN M, A260W)'''<br />
==Overview==
==Overview==
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Anionic lipids play a variety of key roles in biomembrane function, including providing the immediate environment for the integral membrane, proteins that catalyze photosynthetic and respiratory energy transduction., Little is known about the molecular basis of these lipid-protein, interactions. In this study, x-ray crystallography has been used to, examine the structural details of an interaction between cardiolipin and, the photoreaction center, a key light-driven electron transfer protein, complex found in the cytoplasmic membrane of photosynthetic bacteria., X-ray diffraction data collected over the resolution range 30.0-2.1 A show, that binding of the lipid to the protein involves a combination of ionic, interactions between the protein and the lipid headgroup and van der Waals, interactions between the lipid tails and the electroneutral intramembrane, surface of the protein. In the headgroup region, ionic interactions, involve polar groups of a number of residues, the protein backbone, and, bound water molecules. The lipid tails sit along largely hydrophobic, grooves in the irregular surface of the protein. In addition to providing, new information on the immediate lipid environment of a key integral, membrane protein, this study provides the first, to our knowledge, high-resolution x-ray crystal structure for cardiolipin. The possible, significance of this interaction between an integral membrane protein and, cardiolipin is considered.
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Anionic lipids play a variety of key roles in biomembrane function, including providing the immediate environment for the integral membrane proteins that catalyze photosynthetic and respiratory energy transduction. Little is known about the molecular basis of these lipid-protein interactions. In this study, x-ray crystallography has been used to examine the structural details of an interaction between cardiolipin and the photoreaction center, a key light-driven electron transfer protein complex found in the cytoplasmic membrane of photosynthetic bacteria. X-ray diffraction data collected over the resolution range 30.0-2.1 A show that binding of the lipid to the protein involves a combination of ionic interactions between the protein and the lipid headgroup and van der Waals interactions between the lipid tails and the electroneutral intramembrane surface of the protein. In the headgroup region, ionic interactions involve polar groups of a number of residues, the protein backbone, and bound water molecules. The lipid tails sit along largely hydrophobic grooves in the irregular surface of the protein. In addition to providing new information on the immediate lipid environment of a key integral membrane protein, this study provides the first, to our knowledge, high-resolution x-ray crystal structure for cardiolipin. The possible significance of this interaction between an integral membrane protein and cardiolipin is considered.
==About this Structure==
==About this Structure==
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1QOV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with FE2, CL, BCL, BPH, U10, SPN and CDL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QOV OCA].
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1QOV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=BPH:'>BPH</scene>, <scene name='pdbligand=U10:'>U10</scene>, <scene name='pdbligand=SPN:'>SPN</scene> and <scene name='pdbligand=CDL:'>CDL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOV OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Rhodobacter sphaeroides]]
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[[Category: Cogdell, R.J.]]
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[[Category: Cogdell, R J.]]
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[[Category: Fyfe, P.K.]]
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[[Category: Fyfe, P K.]]
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[[Category: Isaacs, N.W.]]
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[[Category: Isaacs, N W.]]
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[[Category: Jones, M.R.]]
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[[Category: Jones, M R.]]
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[[Category: Mcauley, K.E.]]
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[[Category: Mcauley, K E.]]
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[[Category: Ridge, J.P.]]
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[[Category: Ridge, J P.]]
[[Category: BCL]]
[[Category: BCL]]
[[Category: BPH]]
[[Category: BPH]]
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[[Category: transmembrane]]
[[Category: transmembrane]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:51:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:06 2008''

Revision as of 12:42, 21 February 2008

Image:1qov.gif

1qov, resolution 2.1Å

Drag the structure with the mouse to rotate

PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ALA M260 REPLACED WITH TRP (CHAIN M, A260W)

Overview

Anionic lipids play a variety of key roles in biomembrane function, including providing the immediate environment for the integral membrane proteins that catalyze photosynthetic and respiratory energy transduction. Little is known about the molecular basis of these lipid-protein interactions. In this study, x-ray crystallography has been used to examine the structural details of an interaction between cardiolipin and the photoreaction center, a key light-driven electron transfer protein complex found in the cytoplasmic membrane of photosynthetic bacteria. X-ray diffraction data collected over the resolution range 30.0-2.1 A show that binding of the lipid to the protein involves a combination of ionic interactions between the protein and the lipid headgroup and van der Waals interactions between the lipid tails and the electroneutral intramembrane surface of the protein. In the headgroup region, ionic interactions involve polar groups of a number of residues, the protein backbone, and bound water molecules. The lipid tails sit along largely hydrophobic grooves in the irregular surface of the protein. In addition to providing new information on the immediate lipid environment of a key integral membrane protein, this study provides the first, to our knowledge, high-resolution x-ray crystal structure for cardiolipin. The possible significance of this interaction between an integral membrane protein and cardiolipin is considered.

About this Structure

1QOV is a Protein complex structure of sequences from Rhodobacter sphaeroides with , , , , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural details of an interaction between cardiolipin and an integral membrane protein., McAuley KE, Fyfe PK, Ridge JP, Isaacs NW, Cogdell RJ, Jones MR, Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14706-11. PMID:10611277

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