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6jlu

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Revision as of 22:17, 6 March 2020

Structure of PSII-FCP supercomplex from a centric diatom Chaetoceros gracilis at 3.02 angstrom resolution

6jlu, resolution 3.02Å

Structural highlights

6jlu is a 70 chain structure with sequence from Chaetoceros gracilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[B6ZHF4_9STRA] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II.[HAMAP-Rule:MF_01378] [B6ZHF2_9STRA] Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.[HAMAP-Rule:MF_01386] [B7XBY7_9STRA] One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.[HAMAP-Rule:MF_00752]

Publication Abstract from PubMed

Diatoms play important roles in global primary productivity and biogeochemical cycling of carbon, in part owing to the ability of their photosynthetic apparatus to adapt to rapidly changing light intensity. We report a cryo-electron microscopy structure of the photosystem II (PSII)-fucoxanthin (Fx) chlorophyll (Chl) a/c binding protein (FCPII) supercomplex from the centric diatom Chaetoceros gracilis The supercomplex comprises two protomers, each with two tetrameric and three monomeric FCPIIs around a PSII core that contains five extrinsic oxygen-evolving proteins at the lumenal surface. The structure reveals the arrangement of a huge pigment network that contributes to efficient light energy harvesting, transfer, and dissipation processes in the diatoms.

The pigment-protein network of a diatom photosystem II-light-harvesting antenna supercomplex.,Pi X, Zhao S, Wang W, Liu D, Xu C, Han G, Kuang T, Sui SF, Shen JR Science. 2019 Aug 2;365(6452). pii: 365/6452/eaax4406. doi:, 10.1126/science.aax4406. PMID:31371578^[1]

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

References

↑ Pi X, Zhao S, Wang W, Liu D, Xu C, Han G, Kuang T, Sui SF, Shen JR. The pigment-protein network of a diatom photosystem II-light-harvesting antenna supercomplex. Science. 2019 Aug 2;365(6452). pii: 365/6452/eaax4406. doi:, 10.1126/science.aax4406. PMID:31371578 doi:http://dx.doi.org/10.1126/science.aax4406

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/6jlu"

@@ Line 1: / Line 1: @@
 ==Structure of PSII-FCP supercomplex from a centric diatom Chaetoceros gracilis at 3.02 angstrom resolution==
-<StructureSection load='6jlu' size='340' side='right'caption='[[6jlu]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
+<SX load='6jlu' size='340' side='right' viewer='molstar' caption='[[6jlu]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6jlu]] is a 70 chain structure with sequence from [http://en.wikipedia.org/wiki/Chaetoceros_gracilis Chaetoceros gracilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JLU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JLU FirstGlance]. <br>
@@ Line 22: / Line 22: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Chaetoceros gracilis]]
 [[Category: Large Structures]]

6jlu

From Proteopedia

Revision as of 22:17, 6 March 2020

Structure of PSII-FCP supercomplex from a centric diatom Chaetoceros gracilis at 3.02 angstrom resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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