3wmm

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==Crystal structure of the LH1-RC complex from Thermochromatium tepidum in C2 form==
==Crystal structure of the LH1-RC complex from Thermochromatium tepidum in C2 form==
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<StructureSection load='3wmm' size='340' side='right' caption='[[3wmm]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
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<StructureSection load='3wmm' size='340' side='right'caption='[[3wmm]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3wmm]] is a 36 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermochromatium_tepidum Thermochromatium tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WMM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3wmm]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermochromatium_tepidum Thermochromatium tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WMM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=MQ8:MENAQUINONE+8'>MQ8</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene>, <scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.008&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wmn|3wmn]], [[3wmo|3wmo]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=MQ8:MENAQUINONE+8'>MQ8</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene>, <scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmm OCA], [http://pdbe.org/3wmm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wmm RCSB], [http://www.ebi.ac.uk/pdbsum/3wmm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wmm ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wmm OCA], [https://pdbe.org/3wmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wmm RCSB], [https://www.ebi.ac.uk/pdbsum/3wmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wmm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/D2Z0P1_THETI D2Z0P1_THETI]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers (By similarity).[SAAS:SAAS000066_004_008786] [[http://www.uniprot.org/uniprot/D2Z0P5_THETI D2Z0P5_THETI]] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor (By similarity).[PIRNR:PIRNR000017] [[http://www.uniprot.org/uniprot/D2Z0P2_THETI D2Z0P2_THETI]] Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers (By similarity).[SAAS:SAAS000066_004_008786]
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[https://www.uniprot.org/uniprot/CYCR_THETI CYCR_THETI] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.[PIRNR:PIRNR000017]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The light-harvesting core antenna (LH1) and the reaction centre (RC) of purple photosynthetic bacteria form a supramolecular complex (LH1-RC) to use sunlight energy in a highly efficient manner. Here we report the first near-atomic structure, to our knowledge, of a LH1-RC complex, namely that of a Ca2+-bound complex from Thermochromatium tepidum, which reveals detailed information on the arrangement and interactions of the protein subunits and the cofactors. The RC is surrounded by 16 heterodimers of the LH1 alphabeta-subunit that form a completely closed structure. The Ca2+ ions are located at the periplasmic side of LH1. Thirty-two bacteriochlorophyll and 16 spirilloxanthin molecules in the LH1 ring form an elliptical assembly. The geometries of the pigment assembly involved in the absorption characteristics of the bacteriochlorophyll in LH1 and excitation energy transfer among the pigments are reported. In addition, possible ubiquinone channels in the closed LH1 complex are proposed based on the atomic structure.
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Structure of the LH1-RC complex from Thermochromatium tepidum at 3.0 A,Niwa S, Yu LJ, Takeda K, Hirano Y, Kawakami T, Wang-Otomo ZY, Miki K Nature. 2014 Mar 26. doi: 10.1038/nature13197. PMID:24670637<ref>PMID:24670637</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3wmm" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermochromatium tepidum]]
[[Category: Thermochromatium tepidum]]
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[[Category: Miki, K]]
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[[Category: Miki K]]
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[[Category: Niwa, S]]
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[[Category: Niwa S]]
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[[Category: Takeda, K]]
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[[Category: Takeda K]]
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[[Category: Wang-Otomo, Z Y]]
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[[Category: Wang-Otomo Z-Y]]
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[[Category: Photosynthesis]]
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Current revision

Crystal structure of the LH1-RC complex from Thermochromatium tepidum in C2 form

PDB ID 3wmm

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