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| - | [[Image:1nkz.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1nkz.png|left|200px]] |
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| | {{STRUCTURE_1nkz| PDB=1nkz | SCENE= }} | | {{STRUCTURE_1nkz| PDB=1nkz | SCENE= }} |
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| - | '''Crystal structure of LH2 B800-850 from Rps. acidophila at 2.0 Angstrom resolution'''
| + | ===Crystal structure of LH2 B800-850 from Rps. acidophila at 2.0 Angstrom resolution=== |
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| - | ==Overview==
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| - | 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 line below this paragraph, {{ABSTRACT_PUBMED_12595263}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12595263 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12595263}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rhodopin glucoside]] | | [[Category: Rhodopin glucoside]] |
| | [[Category: Trans-membrane helice]] | | [[Category: Trans-membrane helice]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:39:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:54:35 2008'' |
Revision as of 00:54, 29 July 2008
Template:STRUCTURE 1nkz
Crystal structure of LH2 B800-850 from Rps. acidophila at 2.0 Angstrom resolution
Template:ABSTRACT PUBMED 12595263
About this Structure
1NKZ is a Protein complex structure of sequences from Rhodoblastus acidophilus. Full crystallographic information is available from OCA.
Reference
The structure and thermal motion of the B800-850 LH2 complex from Rps.acidophila at 2.0A resolution and 100K: new structural features and functionally relevant motions., Papiz MZ, Prince SM, Howard T, Cogdell RJ, Isaacs NW, J Mol Biol. 2003 Mar 7;326(5):1523-38. PMID:12595263
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