1FC7

PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE

Summary for 1FC7

• Entry DOI: 10.2210/pdb1fc7/pdb
• Related: 1FC6 1FC9 1FCF
• Descriptor: PHOTOSYSTEM II D1 PROTEASE (2 entities in total)
• Functional Keywords: d1 c-terminal processing protease, serine protease, serine-lysine catalytic dyad, pdz domain, photosystem ii, photosynthesis, x-ray crystal structure, hydrolase
• Biological source: Scenedesmus obliquus
• Total number of polymer chains: 1
• Total formula weight: 40749.02

Authors

Liao, D.I.,Qian, J.,Chisholm, D.A.,Jordan, D.B.,Diner, B.A. (deposition date: 2000-07-18, release date: 2001-01-18, Last modification date: 2024-11-06)

Primary citation

Liao, D.I.,Qian, J.,Chisholm, D.A.,Jordan, D.B.,Diner, B.A.
Crystal structures of the photosystem II D1 C-terminal processing protease.
Nat.Struct.Biol., 7:749-753, 2000

PubMed Abstract: 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.

PubMed: 10966643
DOI: 10.1038/78973

Experimental method

X-RAY DIFFRACTION (2 Å)