1mz4
From Proteopedia
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- | [[Image:1mz4.png|left|200px]] | ||
- | + | ==Crystal Structure of Cytochrome c550 from Thermosynechococcus elongatus== | |
+ | <StructureSection load='1mz4' size='340' side='right'caption='[[1mz4]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1mz4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermosynechococcus_vestitus Thermosynechococcus vestitus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZ4 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1mz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mz4 OCA], [https://pdbe.org/1mz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mz4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mz4 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CY550_THEVB CY550_THEVB] One of the extrinsic, lumenal subunits 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. The extrinsic proteins stabilize the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protect the OEC against heat-induced inactivation. Low-potential cytochrome c that plays a role in the OEC of PSII.[HAMAP-Rule:MF_01378]<ref>PMID:11427679</ref> <ref>PMID:20558739</ref> <ref>PMID:21367867</ref> <ref>PMID:25006873</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mz4_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <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/main_output.php?pdb_ID=1mz4 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | First, the crystal structure of cytochrome c-550 (the psbV1 gene product) from the thermophilic cyanobacterium Thermosynechococcus elongatus has been determined to a resolution of 1.8 A. A comparison of the T. elongatus cytochrome c-550 structure to its counterparts from mesophilic organisms, Synechocystis 6803 and Arthrospira maxima, suggests that increased numbers of hydrogen bonds may play a role in the structural basis of thermostability. The cytochrome c-550 in T. elongatus also differs from that in Synechocystis 6803 and Arthrospira maxima in its lack of dimerization and the presence of a trigonal planar molecule, possibly bicarbonate, tightly bound to the heme propionate oxygen atoms. Cytochromes c-550 from T. elongatus, Synechocystis 6803 and Arthrospira maxima exhibit different EPR spectra. A correlation has been done between the heme-axial ligands geometries and the rhombicity calculated from the EPR spectra. This correlation indicates that binding of cytochrome c-550 to Photosystem II is accompanied by structural changes in the heme vicinity. Second, the psbV2 gene product has been found and purified. The UV-visible, EPR and Raman spectra are reported. From the spectroscopic data and from a theoretical structural model based on the cytochrome c-550 structure it is proposed that the 6th ligand of the heme-iron is the Tyr86. | ||
- | + | Structural and EPR characterization of the soluble form of cytochrome c-550 and of the psbV2 gene product from the cyanobacterium Thermosynechococcus elongatus.,Kerfeld CA, Sawaya MR, Bottin H, Tran KT, Sugiura M, Cascio D, Desbois A, Yeates TO, Kirilovsky D, Boussac A Plant Cell Physiol. 2003 Jul;44(7):697-706. PMID:12881497<ref>PMID:12881497</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1mz4" style="background-color:#fffaf0;"></div> | |
- | + | ||
==See Also== | ==See Also== | ||
- | *[[Cytochrome | + | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
- | [[Category: Thermosynechococcus | + | </StructureSection> |
- | [[Category: Bottin | + | [[Category: Large Structures]] |
- | [[Category: Boussac | + | [[Category: Thermosynechococcus vestitus]] |
- | [[Category: Kerfeld | + | [[Category: Bottin H]] |
- | [[Category: Kirilovsky | + | [[Category: Boussac A]] |
- | [[Category: Krogmann | + | [[Category: Kerfeld CA]] |
- | [[Category: Sawaya | + | [[Category: Kirilovsky D]] |
- | [[Category: Sugiura | + | [[Category: Krogmann D]] |
- | [[Category: Tran | + | [[Category: Sawaya MR]] |
- | [[Category: Yeates | + | [[Category: Sugiura M]] |
- | + | [[Category: Tran KT]] | |
- | + | [[Category: Yeates TO]] |
Current revision
Crystal Structure of Cytochrome c550 from Thermosynechococcus elongatus
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