4dgk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:48, 1 March 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dgk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pantoea_ananatis Pantoea ananatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DGK FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dgk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pantoea_ananatis Pantoea ananatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DGK FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=4dgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dgk OCA], [https://pdbe.org/4dgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dgk RCSB], [https://www.ebi.ac.uk/pdbsum/4dgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dgk 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=4dgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dgk OCA], [https://pdbe.org/4dgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dgk RCSB], [https://www.ebi.ac.uk/pdbsum/4dgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dgk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/CRTI_PANAN CRTI_PANAN]] Converts 15-cis-phytoene into all-trans-lycopene via the intermediary of all-trans-phytofluene, all-trans-zeta-carotene and all-trans-neurosporene, by the introduction of four double bonds.<ref>PMID:1400305</ref>
+
[https://www.uniprot.org/uniprot/CRTI_PANAN CRTI_PANAN] Converts 15-cis-phytoene into all-trans-lycopene via the intermediary of all-trans-phytofluene, all-trans-zeta-carotene and all-trans-neurosporene, by the introduction of four double bonds.<ref>PMID:1400305</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
CRTI-type phytoene desaturases prevailing in bacteria and fungi can form lycopene directly from phytoene while plants employ two distinct desaturases and two cis-tans isomerases for the same purpose. This property renders CRTI a valuable gene to engineer provitamin A-formation to help combat vitamin A malnutrition, such as with Golden Rice. To understand the biochemical processes involved, recombinant CRTI was produced and obtained in homogeneous form that shows high enzymatic activity with the lipophilic substrate phytoene contained in phosphatidyl-choline (PC) liposome membranes. The first crystal structure of apo-CRTI reveals that CRTI belongs to the flavoprotein superfamily comprising protoporphyrinogen IX oxidoreductase and monoamine oxidase. CRTI is a membrane-peripheral oxidoreductase which utilizes FAD as the sole redox-active cofactor. Oxygen, replaceable by quinones in its absence, is needed as the terminal electron acceptor. FAD, besides its catalytic role also displays a structural function by enabling the formation of enzymatically active CRTI membrane associates. Under anaerobic conditions the enzyme can act as a carotene cis-trans isomerase. In silico-docking experiments yielded information on substrate binding sites, potential catalytic residues and is in favor of single half-site recognition of the symmetrical C(40) hydrocarbon substrate.
+
-
 
+
-
On the structure and function of the phytoene desaturase CRTI from Pantoea ananatis, a membrane-peripheral and FAD-dependent oxidase/isomerase.,Schaub P, Yu Q, Gemmecker S, Poussin-Courmontagne P, Mailliot J, McEwen AG, Ghisla S, Al-Babili S, Cavarelli J, Beyer P PLoS One. 2012;7(6):e39550. Epub 2012 Jun 22. PMID:22745782<ref>PMID:22745782</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4dgk" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of Phytoene desaturase CRTI from Pantoea ananatis

PDB ID 4dgk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4dgk"
Personal tools