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1fcf

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Revision as of 12:07, 27 April 2022

PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE

Structural highlights

1fcf is a 1 chain structure with sequence from Achnanthes obliqua. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1fc6, 1fc7, 1fc9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CTPA_ACUOB] Protease involved in the C-terminal processing of the chloroplastic D1 protein of photosystem II. This proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.^[1]

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 PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Trost JT, Chisholm DA, Jordan DB, Diner BA. The D1 C-terminal processing protease of photosystem II from Scenedesmus obliquus. Protein purification and gene characterization in wild type and processing mutants. J Biol Chem. 1997 Aug 15;272(33):20348-56. PMID:9252339
↑ Liao DI, Qian J, Chisholm DA, Jordan DB, Diner BA. Crystal structures of the photosystem II D1 C-terminal processing protease. Nat Struct Biol. 2000 Sep;7(9):749-53. PMID:10966643 doi:10.1038/78973

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fcf"

@@ Line 3: / Line 3: @@
 <StructureSection load='1fcf' size='340' side='right'caption='[[1fcf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fcf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Achnanthes_obliqua Achnanthes obliqua]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1FCF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fcf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Achnanthes_obliqua Achnanthes obliqua]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FCF FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fc6|1fc6]], [[1fc7|1fc7]], [[1fc9|1fc9]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fc6|1fc6]], [[1fc7|1fc7]], [[1fc9|1fc9]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1fcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fcf OCA], [http://pdbe.org/1fcf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fcf RCSB], [http://www.ebi.ac.uk/pdbsum/1fcf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fcf 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=1fcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fcf OCA], [https://pdbe.org/1fcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fcf RCSB], [https://www.ebi.ac.uk/pdbsum/1fcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fcf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CTPA_ACUOB CTPA_ACUOB]] Protease involved in the C-terminal processing of the chloroplastic D1 protein of photosystem II. This proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.<ref>PMID:9252339</ref>
+[[https://www.uniprot.org/uniprot/CTPA_ACUOB CTPA_ACUOB]] Protease involved in the C-terminal processing of the chloroplastic D1 protein of photosystem II. This proteolytic processing is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation.<ref>PMID:9252339</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1fcf

From Proteopedia

Revision as of 12:07, 27 April 2022

PHOTOSYSTEM II D1 C-TERMINAL PROCESSING PROTEASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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