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5oy0

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Structure of synechocystis photosystem I trimer at 2.5A resolution

Structural highlights

5oy0 is a 21 chain structure with sequence from Synechocystis sp. PCC 6803. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.501Å
Ligands:	, , , , , , , , , , , , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSAA_SYNY3

Publication Abstract from PubMed

The ability of photosynthetic organisms to use the sun's light as a sole source of energy sustains life on our planet. Photosystems I (PSI) and II (PSII) are large, multi-subunit, pigment-protein complexes that enable photosynthesis, but this intriguing process remains to be explained fully. Currently, crystal structures of these complexes are available for thermophilic prokaryotic cyanobacteria. The mega-Dalton trimeric PSI complex from thermophilic cyanobacterium, Thermosynechococcus elongatus, was solved at 2.5A resolution with X-ray crystallography. That structure revealed the positions of 12 protein subunits (PsaA-F, PsaI-M, and PsaX) and 127 cofactors. Although mesophilic organisms perform most of the world's photosynthesis, no well-resolved trimeric structure of a mesophilic organism exists. Our research model for a mesophilic cyanobacterium was Synechocystis sp. PCC6803. This study aimed to obtain well-resolved crystal structures of [1] a monomeric PSI with all subunits, [2] a trimeric PSI with a reduced number of subunits, and [3] the full, trimeric wild-type PSI complex. We only partially succeeded with the first two structures, but we successfully produced the trimeric PSI structure at 2.5A resolution. This structure was comparable to that of the thermophilic species, but we provided more detail. The PSI trimeric supercomplex consisted of 33 protein subunits, 72 carotenoids, 285 chlorophyll a molecules, 51 lipids, 9 iron-sulfur clusters, 6 plastoquinones, 6 putative calcium ions, and over 870 water molecules. This study showed that the structure of the PSI in Synechocystis sp. PCC6803 differed from previously described PSI structures. These findings have broadened our understanding of PSI structure.

Structure and function of wild-type and subunit-depleted photosystem I in Synechocystis.,Malavath T, Caspy I, Netzer-El SY, Klaiman D, Nelson N Biochim Biophys Acta. 2018 Feb 4. pii: S0005-2728(18)30018-5. doi:, 10.1016/j.bbabio.2018.02.002. PMID:29414678^[1]

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

References

↑ Malavath T, Caspy I, Netzer-El SY, Klaiman D, Nelson N. Structure and function of wild-type and subunit-depleted photosystem I in Synechocystis. Biochim Biophys Acta. 2018 Feb 4. pii: S0005-2728(18)30018-5. doi:, 10.1016/j.bbabio.2018.02.002. PMID:29414678 doi:http://dx.doi.org/10.1016/j.bbabio.2018.02.002

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5oy0"

Categories: Large Structures | Synechocystis sp. PCC 6803 | Caspy I | Malavath T | Nelson N

@@ Line 3: / Line 3: @@
 <StructureSection load='5oy0' size='340' side='right'caption='[[5oy0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5oy0]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp._pcc_6803 Synechocystis sp. pcc 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OY0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OY0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5oy0]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OY0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=45D:BETA,BETA-CAROTENE-4,4-DIONE'>45D</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=ECH:BETA,BETA-CAROTEN-4-ONE'>ECH</scene>, <scene name='pdbligand=EQ3:(3R)-3-HYDROXY-BETA,BETA-CAROTEN-4-ONE'>EQ3</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=ZEX:(3S,5R,6S,3S,5R,6S)+BETA-CAROTENE-3,23-DIOL'>ZEX</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.501&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Photosystem_I Photosystem I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.97.1.12 1.97.1.12] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=45D:BETA,BETA-CAROTENE-4,4-DIONE'>45D</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BCR:BETA-CAROTENE'>BCR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=DGD:DIGALACTOSYL+DIACYL+GLYCEROL+(DGDG)'>DGD</scene>, <scene name='pdbligand=ECH:BETA,BETA-CAROTEN-4-ONE'>ECH</scene>, <scene name='pdbligand=EQ3:(3R)-3-HYDROXY-BETA,BETA-CAROTEN-4-ONE'>EQ3</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PQN:PHYLLOQUINONE'>PQN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=ZEX:(3S,5R,6S,3S,5R,6S)+BETA-CAROTENE-3,23-DIOL'>ZEX</scene></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=5oy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oy0 OCA], [http://pdbe.org/5oy0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oy0 RCSB], [http://www.ebi.ac.uk/pdbsum/5oy0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oy0 ProSAT]</span></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=5oy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oy0 OCA], [https://pdbe.org/5oy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oy0 RCSB], [https://www.ebi.ac.uk/pdbsum/5oy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oy0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PSAE_SYNY3 PSAE_SYNY3]] Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.[HAMAP-Rule:MF_00613]
+[https://www.uniprot.org/uniprot/PSAA_SYNY3 PSAA_SYNY3]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 ==See Also==
-*[[Photosystem I|Photosystem I]]
+*[[Photosystem I 3D structures|Photosystem I 3D structures]]
 == References ==
 <references/>
@@ Line 27: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Photosystem I]]
+[[Category: Synechocystis sp. PCC 6803]]
-[[Category: Synechocystis sp. pcc 6803]]
+[[Category: Caspy I]]
-[[Category: Caspy, I]]
+[[Category: Malavath T]]
-[[Category: Malavath, T]]
+[[Category: Nelson N]]
-[[Category: Nelson, N]]
-[[Category: Cyanobacteria]]
-[[Category: Electron transfer chain]]
-[[Category: Photosynthesis]]
-[[Category: Photosystem i]]
-[[Category: Reaction center]]
-[[Category: Synechocysti]]

5oy0

From Proteopedia

Current revision

Structure of synechocystis photosystem I trimer at 2.5A resolution

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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