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| | <StructureSection load='5b5m' size='340' side='right'caption='[[5b5m]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='5b5m' size='340' side='right'caption='[[5b5m]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b5m]] is a 72 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=5B5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B5M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b5m]] is a 72 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=5B5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B5M FirstGlance]. <br> |
| - | </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=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=SR:STRONTIUM+ION'>SR</scene>, <scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</scene></td></tr> | + | </td></tr><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=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=SR:STRONTIUM+ION'>SR</scene>, <scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b5n|5b5n]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b5m OCA], [https://pdbe.org/5b5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b5m RCSB], [https://www.ebi.ac.uk/pdbsum/5b5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b5m ProSAT]</span></td></tr> |
| - | <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=5b5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b5m OCA], [http://pdbe.org/5b5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b5m RCSB], [http://www.ebi.ac.uk/pdbsum/5b5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b5m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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] | + | [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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Thermochromatium tepidum]] | | [[Category: Thermochromatium tepidum]] |
| - | [[Category: Wang-Otomo, Z Y]] | + | [[Category: Wang-Otomo Z-Y]] |
| - | [[Category: Yu, L J]] | + | [[Category: Yu L-J]] |
| - | [[Category: Bacterial photosynthesis]]
| + | |
| - | [[Category: Light-harvesting complex]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| Structural highlights
5b5m is a 72 chain structure with sequence from Thermochromatium tepidum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
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]
Publication Abstract from PubMed
While the majority of the core light-harvesting complexes (LH1) in purple photosynthetic bacteria exhibit a Qy absorption band in the range of 870-890 nm, LH1 from the thermophilic bacterium Thermochromatium tepidum displays the Qy band at 915 nm with an enhanced thermostability. These properties are regulated by Ca2+ ions. Substitution of the Ca2+ with other divalent metal ions results in a complex with the Qy band blue-shifted to 880-890 nm and a reduced thermostability. Following the recent publication of the structure of the Ca-bound LH1-reaction center (RC) complex [Niwa, S., et al. (2014) Nature 508, 228], we have determined the crystal structures of the Sr- and Ba-substituted LH1-RC complexes with the LH1 Qy band at 888 nm. Sixteen Sr2+ and Ba2+ ions are identified in the LH1 complexes. Both Sr2+ and Ba2+ are located at the same positions, and these are clearly different from, though close to, the Ca2+-binding sites. Conformational rearrangement induced by the substitution is limited to the metal-binding sites. Unlike the Ca-LH1-RC complex, only the alpha-polypeptides are involved in the Sr and Ba coordinations in LH1. The difference in the thermostability between these complexes can be attributed to the different patterns of the network formed by metal binding. The Sr- and Ba-LH1-RC complexes form a single-ring network by the LH1 alpha-polypeptides only, in contrast to the double-ring network composed of both alpha- and beta-polypeptides in the Ca-LH1-RC complex. On the basis of the structural information, a combined effect of hydrogen bonding, structural integrity, and charge distribution is considered to influence the spectral properties of the core antenna complex.
Structural Basis for the Unusual Qy Red-Shift and Enhanced Thermostability of the LH1 Complex from Thermochromatium tepidum.,Yu LJ, Kawakami T, Kimura Y, Wang-Otomo ZY Biochemistry. 2016 Nov 29;55(47):6495-6504. Epub 2016 Nov 16. PMID:27933779[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yu LJ, Kawakami T, Kimura Y, Wang-Otomo ZY. Structural Basis for the Unusual Qy Red-Shift and Enhanced Thermostability of the LH1 Complex from Thermochromatium tepidum. Biochemistry. 2016 Nov 29;55(47):6495-6504. Epub 2016 Nov 16. PMID:27933779 doi:http://dx.doi.org/10.1021/acs.biochem.6b00742
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