1fcf: Difference between revisions

Revision as of 03:02, 1 July 2008

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File:1fcf.png

Template:STRUCTURE 1fcf

PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASEPHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE

Template:ABSTRACT PUBMED 10966643

About this StructureAbout this Structure

1FCF is a Single protein structure of sequence from Scenedesmus obliquus. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 03:02:38 2008

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OCA

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-'''PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE'''
+===PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE===
-==Overview==
+<!--
-We 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10966643}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10966643 is the PubMed ID number.
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 [[Category: Serine-lysine catalytic dyad]]
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