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3a0b

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Revision as of 21:51, 5 August 2016

Crystal structure of Br-substituted Photosystem II complex

Structural highlights

3a0b is a 40 chain structure with sequence from Thermosynechococcus vulcanus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , , , , ,
NonStd Res:
Related:	3a0h
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PSBF_THEVL] This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00643] [PSBL_THEVL] This protein is a component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01317] [PSBJ_THEVL] This protein is a component of the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01305] [PSBT_THEVL] Seems to play a role in the dimerization of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00808] [PSBA_THEVL] D1 (PsbA) and D2 (PsbD) bind P680, the primary electron donor of photosystem II (PSII) as well as electron acceptors. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_01379] [CY550_THEVL] Low-potential cytochrome c that plays a role in the oxygen-evolving complex of photosystem II (PSII). Binds to PSII in the absence of other extrinsic proteins; required for binding of the PsbU protein to photosystem II. In PSII particles without oxygen-evolving activity, maximal activity is restored only by binding of cytochrome c550, PsbU and the 33 kDa PsbO protein. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.^[1] ^[2] [PSBE_THEVL] This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.[HAMAP-Rule:MF_00642]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The chloride ion, Cl(-), is an essential cofactor for oxygen evolution of photosystem II (PSII) and is closely associated with the Mn(4)Ca cluster. Its detailed location and function have not been identified, however. We substituted Cl(-) with a bromide ion (Br(-)) or an iodide ion (I(-)) in PSII and analyzed the crystal structures of PSII with Br(-) and I(-) substitutions. Substitution of Cl(-) with Br(-) did not inhibit oxygen evolution, whereas substitution of Cl(-) with I(-) completely inhibited oxygen evolution, indicating the efficient replacement of Cl(-) by I(-). PSII with Br(-) and I(-) substitutions were crystallized, and their structures were analyzed. The results showed that there are 2 anion-binding sites in each PSII monomer; they are located on 2 sides of the Mn(4)Ca cluster at equal distances from the metal cluster. Anion-binding site 1 is close to the main chain of D1-Glu-333, and site 2 is close to the main chain of CP43-Glu-354; these 2 residues are coordinated directly with the Mn(4)Ca cluster. In addition, site 1 is located in the entrance of a proton exit channel. These results indicate that these 2 Cl(-) anions are required to maintain the coordination structure of the Mn(4)Ca cluster as well as the proposed proton channel, thereby keeping the oxygen-evolving complex fully active.

Location of chloride and its possible functions in oxygen-evolving photosystem II revealed by X-ray crystallography.,Kawakami K, Umena Y, Kamiya N, Shen JR Proc Natl Acad Sci U S A. 2009 May 26;106(21):8567-72. Epub 2009 May 11. PMID:19433803^[3]

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

References

↑ Shen JR, Ikeuchi M, Inoue Y. Stoichiometric association of extrinsic cytochrome c550 and 12 kDa protein with a highly purified oxygen-evolving photosystem II core complex from Synechococcus vulcanus. FEBS Lett. 1992 Apr 20;301(2):145-9. PMID:1314738
↑ Shen JR, Inoue Y. Binding and functional properties of two new extrinsic components, cytochrome c-550 and a 12-kDa protein, in cyanobacterial photosystem II. Biochemistry. 1993 Feb 23;32(7):1825-32. PMID:8382523
↑ Kawakami K, Umena Y, Kamiya N, Shen JR. Location of chloride and its possible functions in oxygen-evolving photosystem II revealed by X-ray crystallography. Proc Natl Acad Sci U S A. 2009 May 26;106(21):8567-72. Epub 2009 May 11. PMID:19433803

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3a0b"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Br-substituted Photosystem II complex==
 <StructureSection load='3a0b' size='340' side='right' caption='[[3a0b]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a0h|3a0h]]</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=3a0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a0b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a0b RCSB], [http://www.ebi.ac.uk/pdbsum/3a0b 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=3a0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a0b OCA], [http://pdbe.org/3a0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a0b RCSB], [http://www.ebi.ac.uk/pdbsum/3a0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a0b ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a0b ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 28: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3a0b" style="background-color:#fffaf0;"></div>
 ==See Also==

3a0b

From Proteopedia

Revision as of 21:51, 5 August 2016

Crystal structure of Br-substituted Photosystem II complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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