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==Cytochrome b6f Complex Crystal Structure from Mastigocladus laminosus with n-Side Inhibitor NQNO== | |||
<StructureSection load='4h0l' size='340' side='right'caption='[[4h0l]], [[Resolution|resolution]] 3.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4h0l]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mastigocladus_laminosus Mastigocladus laminosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H0L FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=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=QNO:2-NONYL-4-HYDROXYQUINOLINE+N-OXIDE'>QNO</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4h0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h0l OCA], [https://pdbe.org/4h0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h0l RCSB], [https://www.ebi.ac.uk/pdbsum/4h0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h0l ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UCRI_MASLA UCRI_MASLA] 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. | |||
<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> | |||
<div class="pdbe-citations 4h0l" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome b6|Cytochrome b6]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mastigocladus laminosus]] | |||
[[Category: Baniulis D]] | |||
[[Category: Cramer WA]] | |||
[[Category: Hasan SS]] | |||
[[Category: Yamashita E]] | |||
Latest revision as of 13:03, 30 October 2024
Cytochrome b6f Complex Crystal Structure from Mastigocladus laminosus with n-Side Inhibitor NQNOCytochrome b6f Complex Crystal Structure from Mastigocladus laminosus with n-Side Inhibitor NQNO
Structural highlights
FunctionUCRI_MASLA 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. Publication Abstract from PubMedAs 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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