1eys

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|PDB= 1eys |SIZE=350|CAPTION= <scene name='initialview01'>1eys</scene>, resolution 2.2&Aring;
|PDB= 1eys |SIZE=350|CAPTION= <scene name='initialview01'>1eys</scene>, resolution 2.2&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=MQ8:MENAQUINONE+8'>MQ8</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=CRT:SPIRILLOXANTHIN'>CRT</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene> and <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene>
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|LIGAND= <scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CRT:SPIRILLOXANTHIN'>CRT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MQ8:MENAQUINONE+8'>MQ8</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eys OCA], [http://www.ebi.ac.uk/pdbsum/1eys PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eys RCSB]</span>
}}
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[[Category: Nogi, T.]]
[[Category: Nogi, T.]]
[[Category: Nozawa, T.]]
[[Category: Nozawa, T.]]
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[[Category: BCL]]
 
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[[Category: BGL]]
 
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[[Category: BPH]]
 
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[[Category: CRT]]
 
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[[Category: FE]]
 
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[[Category: HEM]]
 
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[[Category: LDA]]
 
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[[Category: MQ8]]
 
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[[Category: PEF]]
 
[[Category: membrane protein complex]]
[[Category: membrane protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:02:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:12:22 2008''

Revision as of 17:12, 30 March 2008


PDB ID 1eys

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: , , , , , , , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF PHOTOSYNTHETIC REACTION CENTER FROM A THERMOPHILIC BACTERIUM, THERMOCHROMATIUM TEPIDUM


Overview

The reaction center (RC) of photosynthetic bacteria is a membrane protein complex that promotes a light-induced charge separation during the primary process of photosynthesis. In the photosynthetic electron transfer chain, the soluble electron carrier proteins transport electrons to the RC and reduce the photo-oxidized special-pair of bacteriochlorophyll. The high-potential iron-sulfur protein (HiPIP) is known to serve as an electron donor to the RC in some species, where the c-type cytochrome subunit, the peripheral subunit of the RC, directly accepts electrons from the HiPIP. Here we report the crystal structures of the RC and the HiPIP from Thermochromatium (Tch.) tepidum, at 2.2-A and 1.5-A resolution, respectively. Tch. tepidum can grow at the highest temperature of all known purple bacteria, and the Tch. tepidum RC shows some degree of stability to high temperature. Comparison with the RCs of mesophiles, such as Blastochloris viridis, has shown that the Tch. tepidum RC possesses more Arg residues at the membrane surface, which might contribute to the stability of this membrane protein. The RC and the HiPIP both possess hydrophobic patches on their respective surfaces, and the HiPIP is expected to interact with the cytochrome subunit by hydrophobic interactions near the heme-1, the most distal heme to the special-pair.

About this Structure

1EYS is a Single protein structure of sequence from Thermochromatium tepidum. Full crystallographic information is available from OCA.

Reference

Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer., Nogi T, Fathir I, Kobayashi M, Nozawa T, Miki K, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13561-6. PMID:11095707

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