4ri3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ri3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RI3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ri3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RI3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=DCW:DICYCLOHEXYLUREA'>DCW</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 2.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=DCW:DICYCLOHEXYLUREA'>DCW</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=4ri3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri3 OCA], [https://pdbe.org/4ri3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ri3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ri3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri3 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=4ri3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ri3 OCA], [https://pdbe.org/4ri3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ri3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ri3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ri3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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==See Also== | ==See Also== | ||
*[[Photosystem II|Photosystem II]] | *[[Photosystem II 3D structures|Photosystem II 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 10:21, 27 November 2024
Crystal structure of DCCD-modified PsbS from spinachCrystal structure of DCCD-modified PsbS from spinach
Structural highlights
FunctionPSBS_SPIOL Seems to be involved in non-photochemical quenching, a process maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage. Publication Abstract from PubMedThe photosystem II protein PsbS has an essential role in qE-type nonphotochemical quenching, which protects plants from photodamage under excess light conditions. qE is initiated by activation of PsbS by low pH, but the mechanism of PsbS action remains elusive. Here we report the low-pH crystal structures of PsbS from spinach in its free form and in complex with the qE inhibitor N,N'-dicyclohexylcarbodiimide (DCCD), revealing that PsbS adopts a unique folding pattern, and, unlike other members of the light-harvesting-complex superfamily, it is a noncanonical pigment-binding protein. Structural and biochemical evidence shows that both active and inactive PsbS form homodimers in the thylakoid membranes, and DCCD binding disrupts the lumenal intermolecular hydrogen bonds of the active PsbS dimer. Activation of PsbS by low pH during qE may involve a conformational change associated with altered lumenal intermolecular interactions of the PsbS dimer. Crystal structures of the PsbS protein essential for photoprotection in plants.,Fan M, Li M, Liu Z, Cao P, Pan X, Zhang H, Zhao X, Zhang J, Chang W Nat Struct Mol Biol. 2015 Aug 10. doi: 10.1038/nsmb.3068. PMID:26258636[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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