1fc6: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fc6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acutodesmus_obliquus Acutodesmus obliquus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FC6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fc6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acutodesmus_obliquus Acutodesmus obliquus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FC6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FC6 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fc7|1fc7]], [[1fc9|1fc9]], [[1fcf|1fcf]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fc7|1fc7]], [[1fc9|1fc9]], [[1fcf|1fcf]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fc6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fc6 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=1fc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fc6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fc6 RCSB], [http://www.ebi.ac.uk/pdbsum/1fc6 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Acutodesmus obliquus]] | [[Category: Acutodesmus obliquus]] | ||
[[Category: Chisholm, D A | [[Category: Chisholm, D A]] | ||
[[Category: Diner, B A | [[Category: Diner, B A]] | ||
[[Category: Jordan, D B | [[Category: Jordan, D B]] | ||
[[Category: Liao, D I | [[Category: Liao, D I]] | ||
[[Category: Qian, J | [[Category: Qian, J]] | ||
[[Category: D1 c-terminal processing protease]] | [[Category: D1 c-terminal processing protease]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 02:35, 23 December 2014
PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASEPHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE
Structural highlights
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 PubMedWe report here the first three-dimensional structure of the D1 C-terminal processing protease (D1P), which is encoded by the ctpA gene. This enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II of oxygenic photosynthesis. Proteolytic processing is necessary to allow the light driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. The X-ray structure of the Scenedesmus obliquus enzyme has been determined at 1.8 A resolution using the multiwavelength anomalous dispersion method. The enzyme is monomeric and is composed of three folding domains. The middle domain is topologically homologous to known PDZ motifs and is proposed to be the site at which the substrate C-terminus binds. The remainder of the substrate likely extends across the face of the enzyme, interacting at its scissile bond with the enzyme active site Ser 372 / Lys 397 catalytic dyad, which lies at the center of the protein at the interface of the three domains. Crystal structures of the photosystem II D1 C-terminal processing protease.,Liao DI, Qian J, Chisholm DA, Jordan DB, Diner BA Nat Struct Biol. 2000 Sep;7(9):749-53. PMID:10966643[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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