4h44
From Proteopedia
(Difference between revisions)
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| - | + | ==2.70 A Cytochrome b6f Complex Structure From Nostoc PCC 7120== | |
| - | + | <StructureSection load='4h44' size='340' side='right' caption='[[4h44]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4h44]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H44 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H44 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7PH:(1R)-2-(DODECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+TETRADECANOATE'>7PH</scene>, <scene name='pdbligand=8K6:OCTADECANE'>8K6</scene>, <scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MYS:PENTADECANE'>MYS</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=OPC:(7R,17E)-4-HYDROXY-N,N,N,7-TETRAMETHYL-7-[(8E)-OCTADEC-8-ENOYLOXY]-10-OXO-3,5,9-TRIOXA-4-PHOSPHAHEPTACOS-17-EN-1-AMINIUM+4-OXIDE'>OPC</scene>, <scene name='pdbligand=SQD:1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL'>SQD</scene>, <scene name='pdbligand=UMQ:UNDECYL-MALTOSIDE'>UMQ</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4h0l|4h0l]], [[4h13|4h13]], [[2zt9|2zt9]], [[2e74|2e74]], [[2e75|2e75]], [[2e76|2e76]], [[1vf5|1vf5]], [[2d2c|2d2c]], [[1q90|1q90]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Plastoquinol--plastocyanin_reductase Plastoquinol--plastocyanin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.9.1 1.10.9.1] </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=4h44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h44 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h44 RCSB], [http://www.ebi.ac.uk/pdbsum/4h44 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/PETM_NOSS1 PETM_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/CYF_NOSS1 CYF_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/PETG_NOSS1 PETG_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex (By similarity). [[http://www.uniprot.org/uniprot/PETD_NOSS1 PETD_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/PETN_NOSS1 PETN_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/CYB6_NOSS1 CYB6_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/UCRIA_NOSS1 UCRIA_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/PETL_NOSS1 PETL_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex (By similarity). | [[http://www.uniprot.org/uniprot/PETM_NOSS1 PETM_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/CYF_NOSS1 CYF_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/PETG_NOSS1 PETG_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex (By similarity). [[http://www.uniprot.org/uniprot/PETD_NOSS1 PETD_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/PETN_NOSS1 PETN_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/CYB6_NOSS1 CYB6_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/UCRIA_NOSS1 UCRIA_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions (By similarity). [[http://www.uniprot.org/uniprot/PETL_NOSS1 PETL_NOSS1]] Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | As much as two-thirds of the proton gradient used for transmembrane free energy storage in oxygenic photosynthesis is generated by the cytochrome bf complex. The proton uptake pathway from the electrochemically negative (n) aqueous phase to the n-side quinone binding site of the complex, and a probable route for proton exit to the positive phase resulting from quinol oxidation, are defined in a 2.70-A crystal structure and in structures with quinone analog inhibitors at 3.07 A (tridecyl-stigmatellin) and 3.25-A (2-nonyl-4-hydroxyquinoline N-oxide) resolution. The simplest n-side proton pathway extends from the aqueous phase via Asp20 and Arg207 (cytochrome b subunit) to quinone bound axially to heme c. On the positive side, the heme-proximal Glu78 (subunit IV), which accepts protons from plastosemiquinone, defines a route for H transfer to the aqueous phase. These pathways provide a structure-based description of the quinone-mediated proton transfer responsible for generation of the transmembrane electrochemical potential gradient in oxygenic photosynthesis. | ||
| + | |||
| + | Quinone-dependent proton transfer pathways in the photosynthetic cytochrome b6f complex.,Hasan SS, Yamashita E, Baniulis D, Cramer WA Proc Natl Acad Sci U S A. 2013 Mar 12;110(11):4297-302. doi:, 10.1073/pnas.1222248110. Epub 2013 Feb 25. PMID:23440205<ref>PMID:23440205</ref> | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Anabaena 7120]] | ||
[[Category: Plastoquinol--plastocyanin reductase]] | [[Category: Plastoquinol--plastocyanin reductase]] | ||
| - | [[Category: Baniulis, D | + | [[Category: Baniulis, D]] |
| - | [[Category: Cramer, W A | + | [[Category: Cramer, W A]] |
| - | [[Category: Hasan, S S | + | [[Category: Hasan, S S]] |
| - | [[Category: Yamashita, E | + | [[Category: Yamashita, E]] |
[[Category: Alpha helix]] | [[Category: Alpha helix]] | ||
[[Category: Beta-sheet]] | [[Category: Beta-sheet]] | ||
Revision as of 02:03, 25 December 2014
2.70 A Cytochrome b6f Complex Structure From Nostoc PCC 7120
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