1nkz: Difference between revisions

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[[Image:1nkz.gif|left|200px]]<br /><applet load="1nkz" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1nkz.gif|left|200px]]<br /><applet load="1nkz" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1nkz, resolution 2.00Å" />

'''Crystal structure of LH2 B800-850 from Rps. acidophila at 2.0 Angstrom resolution'''<br />

==Overview==

The structure at 100K of integral membrane light-harvesting complex II, (LH2) from Rhodopseudomonas acidophila strain 10050 has been refined to, 2.0A resolution. The electron density has been significantly improved, compared to the 2.5A resolution map, by high resolution data, cryo-cooling, and translation, libration, screw (TLS) refinement. The electron density, reveals a second carotenoid molecule, the last five C-terminal residues of, the alpha-chain and a carboxy modified alpha-Met1 which forms the ligand, of the B800 bacteriochlorophyll. TLS refinement has enabled the, characterisation of displacements between molecules in the complex. B850, bacteriochlorophyll molecules are arranged in a ring of 18 pigments, composed of nine approximate dimers. These pigments are strongly coupled, and at their equilibrium positions the excited state dipole interaction, energies, within and between dimers, are approximately 370cm(-1) and, 280cm(-1), respectively. This difference in coupling energy is similar in, magnitude to changes in interaction energies arising from the pigment, displacements described by TLS tensors. The displacements appear to be, non-random in nature and appear to be designed to optimise the modulation, of pigment energy interactions. This is the first time that LH2 pigment, displacements have been quantified experimentally. The calculated energy, changes indicate that there may be significant contributions to, inter-pigment energy interactions from molecular displacements and these, may be of importance to photosynthetic energy transfer.

The structure at 100K of integral membrane light-harvesting complex II (LH2) from Rhodopseudomonas acidophila strain 10050 has been refined to 2.0A resolution. The electron density has been significantly improved, compared to the 2.5A resolution map, by high resolution data, cryo-cooling and translation, libration, screw (TLS) refinement. The electron density reveals a second carotenoid molecule, the last five C-terminal residues of the alpha-chain and a carboxy modified alpha-Met1 which forms the ligand of the B800 bacteriochlorophyll. TLS refinement has enabled the characterisation of displacements between molecules in the complex. B850 bacteriochlorophyll molecules are arranged in a ring of 18 pigments composed of nine approximate dimers. These pigments are strongly coupled and at their equilibrium positions the excited state dipole interaction energies, within and between dimers, are approximately 370cm(-1) and 280cm(-1), respectively. This difference in coupling energy is similar in magnitude to changes in interaction energies arising from the pigment displacements described by TLS tensors. The displacements appear to be non-random in nature and appear to be designed to optimise the modulation of pigment energy interactions. This is the first time that LH2 pigment displacements have been quantified experimentally. The calculated energy changes indicate that there may be significant contributions to inter-pigment energy interactions from molecular displacements and these may be of importance to photosynthetic energy transfer.

==About this Structure==

1NKZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodoblastus_acidophilus Rhodoblastus acidophilus] with RG1, BOG, BCL and BEN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1NKZ OCA].

1NKZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodoblastus_acidophilus Rhodoblastus acidophilus] with <scene name='pdbligand=RG1:'>RG1</scene>, <scene name='pdbligand=BOG:'>BOG</scene>, <scene name='pdbligand=BCL:'>BCL</scene> and <scene name='pdbligand=BEN:'>BEN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKZ OCA].

==Reference==

Line 13:

[[Category: Protein complex]]

[[Category: Rhodoblastus acidophilus]]

[[Category: Cogdell, R.J.]]

[[Category: Cogdell, R J.]]

[[Category: Howard, T]]

[[Category: Isaacs, N.W.]]

[[Category: Isaacs, N W.]]

[[Category: Papiz, M.Z.]]

[[Category: Papiz, M Z.]]

[[Category: Prince, S.M.]]

[[Category: Prince, S M.]]

[[Category: BCL]]

[[Category: BEN]]

Line 29:

[[Category: trans-membrane helices]]

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@@ Line 1: / Line 1: @@
-[[Image:1nkz.gif|left|200px]]<br /><applet load="1nkz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1nkz.gif|left|200px]]<br /><applet load="1nkz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1nkz, resolution 2.00&Aring;" />
 '''Crystal structure of LH2 B800-850 from Rps. acidophila at 2.0 Angstrom resolution'''<br />
 ==Overview==
-The structure at 100K of integral membrane light-harvesting complex II, (LH2) from Rhodopseudomonas acidophila strain 10050 has been refined to, 2.0A resolution. The electron density has been significantly improved, compared to the 2.5A resolution map, by high resolution data, cryo-cooling, and translation, libration, screw (TLS) refinement. The electron density, reveals a second carotenoid molecule, the last five C-terminal residues of, the alpha-chain and a carboxy modified alpha-Met1 which forms the ligand, of the B800 bacteriochlorophyll. TLS refinement has enabled the, characterisation of displacements between molecules in the complex. B850, bacteriochlorophyll molecules are arranged in a ring of 18 pigments, composed of nine approximate dimers. These pigments are strongly coupled, and at their equilibrium positions the excited state dipole interaction, energies, within and between dimers, are approximately 370cm(-1) and, 280cm(-1), respectively. This difference in coupling energy is similar in, magnitude to changes in interaction energies arising from the pigment, displacements described by TLS tensors. The displacements appear to be, non-random in nature and appear to be designed to optimise the modulation, of pigment energy interactions. This is the first time that LH2 pigment, displacements have been quantified experimentally. The calculated energy, changes indicate that there may be significant contributions to, inter-pigment energy interactions from molecular displacements and these, may be of importance to photosynthetic energy transfer.
+The structure at 100K of integral membrane light-harvesting complex II (LH2) from Rhodopseudomonas acidophila strain 10050 has been refined to 2.0A resolution. The electron density has been significantly improved, compared to the 2.5A resolution map, by high resolution data, cryo-cooling and translation, libration, screw (TLS) refinement. The electron density reveals a second carotenoid molecule, the last five C-terminal residues of the alpha-chain and a carboxy modified alpha-Met1 which forms the ligand of the B800 bacteriochlorophyll. TLS refinement has enabled the characterisation of displacements between molecules in the complex. B850 bacteriochlorophyll molecules are arranged in a ring of 18 pigments composed of nine approximate dimers. These pigments are strongly coupled and at their equilibrium positions the excited state dipole interaction energies, within and between dimers, are approximately 370cm(-1) and 280cm(-1), respectively. This difference in coupling energy is similar in magnitude to changes in interaction energies arising from the pigment displacements described by TLS tensors. The displacements appear to be non-random in nature and appear to be designed to optimise the modulation of pigment energy interactions. This is the first time that LH2 pigment displacements have been quantified experimentally. The calculated energy changes indicate that there may be significant contributions to inter-pigment energy interactions from molecular displacements and these may be of importance to photosynthetic energy transfer.
 ==About this Structure==
-NKZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodoblastus_acidophilus Rhodoblastus acidophilus] with RG1, BOG, BCL and BEN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NKZ OCA].
+NKZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodoblastus_acidophilus Rhodoblastus acidophilus] with <scene name='pdbligand=RG1:'>RG1</scene>, <scene name='pdbligand=BOG:'>BOG</scene>, <scene name='pdbligand=BCL:'>BCL</scene> and <scene name='pdbligand=BEN:'>BEN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKZ OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Rhodoblastus acidophilus]]
-[[Category: Cogdell, R.J.]]
+[[Category: Cogdell, R J.]]
 [[Category: Howard, T]]
-[[Category: Isaacs, N.W.]]
+[[Category: Isaacs, N W.]]
-[[Category: Papiz, M.Z.]]
+[[Category: Papiz, M Z.]]
-[[Category: Prince, S.M.]]
+[[Category: Prince, S M.]]
 [[Category: BCL]]
 [[Category: BEN]]
@@ Line 29: / Line 29: @@
 [[Category: trans-membrane helices]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:21:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:13 2008''