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4pv1

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Revision as of 16:05, 11 August 2016

Cytochrome B6F structure from M. laminosus with the quinone analog inhibitor stigmatellin

Structural highlights

4pv1 is a 8 chain structure with sequence from Mastigocladus laminosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , , , , , ,
Related:	1vf5, 1q90, 2e74, 2e75, 2e76, 2zt9, 4h44, 4h13, 4h0l, 3cx5, 4ogq
Activity:	Plastoquinol--plastocyanin reductase, with EC number 1.10.9.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PETM_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. [CYF_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. [PETG_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. PetG is required for either the stability or assembly of the cytochrome b6-f complex. [PETD_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. [PETN_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. [CYB6_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.[HAMAP-Rule:MF_00633] [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. [PETL_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. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.

Publication Abstract from PubMed

The cytochrome bc complexes b6f and bc1 catalyze proton-coupled quinol/quinone redox reactions to generate a transmembrane proton electrochemical gradient. Quinol oxidation on the electrochemically positive (p) interface of the complex occurs at the end of a narrow quinol/quinone entry/exit Qp portal, 11 A long in bc complexes. Superoxide, which has multiple signaling functions, is a by-product of the p-side quinol oxidation. Although the transmembrane core and the chemistry of quinone redox reactions are conserved in bc complexes, the rate of superoxide generation is an order of magnitude greater in the b6f complex, implying that functionally significant differences in structure exist between the b6f and bc1 complexes on the p-side. A unique structure feature of the b6f p-side quinol oxidation site is the presence of a single chlorophyll-a molecule whose function is unrelated to light harvesting. This study describes a cocrystal structure of the cytochrome b6f complex with the quinol analog stigmatellin, which partitions in the Qp portal of the bc1 complex, but not effectively in b6f. It is inferred that the Qp portal is partially occluded in the b6f complex relative to bc1. Based on a discrete molecular-dynamics analysis, occlusion of the Qp portal is attributed to the presence of the chlorophyll phytyl tail, which increases the quinone residence time within the Qp portal and is inferred to be a cause of enhanced superoxide production. This study attributes a novel (to our knowledge), structure-linked function to the otherwise enigmatic chlorophyll-a in the b6f complex, which may also be relevant to intracellular redox signaling.

Traffic within the cytochrome b6f lipoprotein complex: gating of the quinone portal.,Hasan SS, Proctor EA, Yamashita E, Dokholyan NV, Cramer WA Biophys J. 2014 Oct 7;107(7):1620-8. doi: 10.1016/j.bpj.2014.08.003. PMID:25296314^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hasan SS, Proctor EA, Yamashita E, Dokholyan NV, Cramer WA. Traffic within the cytochrome b6f lipoprotein complex: gating of the quinone portal. Biophys J. 2014 Oct 7;107(7):1620-8. doi: 10.1016/j.bpj.2014.08.003. PMID:25296314 doi:http://dx.doi.org/10.1016/j.bpj.2014.08.003

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4pv1"

@@ Line 1: / Line 1: @@
 ==Cytochrome B6F structure from M. laminosus with the quinone analog inhibitor stigmatellin==
 <StructureSection load='4pv1' size='340' side='right' caption='[[4pv1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vf5|1vf5]], [[1q90|1q90]], [[2e74|2e74]], [[2e75|2e75]], [[2e76|2e76]], [[2zt9|2zt9]], [[4h44|4h44]], [[4h13|4h13]], [[4h0l|4h0l]], [[3cx5|3cx5]], [[4ogq|4ogq]]</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=4pv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pv1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pv1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pv1 PDBsum]</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=4pv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pv1 OCA], [http://pdbe.org/4pv1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pv1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pv1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pv1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4pv1" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4pv1

From Proteopedia

Revision as of 16:05, 11 August 2016

Cytochrome B6F structure from M. laminosus with the quinone analog inhibitor stigmatellin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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