1sez

<table><tr><td colspan='2'>[[1sez]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/American_tobacco American tobacco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SEZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SEZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=OMN:4-BROMO-3-(5-CARBOXY-4-CHLORO-2-FLUOROPHENYL)-1-METHYL-5-TRIFLUOROMETHYL-PYRAZOL'>OMN</scene>, <scene name='pdbligand=TON:2-{2-[4-(1,1,3,3-TETRAMETHYLBUTYL)PHENOXY]ETHOXY}ETHANOL'>TON</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protoporphyrinogen_oxidase Protoporphyrinogen oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.3.4 1.3.3.4] </span></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=1sez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sez OCA], [http://pdbe.org/1sez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sez RCSB], [http://www.ebi.ac.uk/pdbsum/1sez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sez ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PPOM_TOBAC PPOM_TOBAC]] Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.<ref>PMID:9238074</ref> Provides precursor for the mitochondrial and plastidic heme synthesis and the predominant chlorophyll synthesis in plastids.<ref>PMID:9238074</ref>

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== Publication Abstract from PubMed ==

Protoporphyrinogen IX oxidase (PPO), the last common enzyme of haem and chlorophyll biosynthesis, catalyses the oxidation of protoporphyrinogen IX to protoporphyrin IX. The membrane-embedded flavoprotein is the target of a large class of herbicides. In humans, a defect in PPO is responsible for the dominantly inherited disease variegate porphyria. Here we present the crystal structure of mitochondrial PPO from tobacco complexed with a phenyl-pyrazol inhibitor. PPO forms a loosely associated dimer and folds into an FAD-binding domain of the p-hydroxybenzoate-hydrolase fold and a substrate-binding domain that enclose a narrow active site cavity beneath the FAD and an alpha-helical membrane-binding domain. The active site architecture suggests a specific substrate-binding mode compatible with the unusual six-electron oxidation. The membrane-binding domains can be docked onto the dimeric structure of human ferrochelatase, the next enzyme in haem biosynthesis, embedded in the opposite side of the membrane. This modelled transmembrane complex provides a structural explanation for the uncoupling of haem biosynthesis observed in variegate porphyria patients and in plants after inhibiting PPO.

Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis.,Koch M, Breithaupt C, Kiefersauer R, Freigang J, Huber R, Messerschmidt A EMBO J. 2004 Apr 21;23(8):1720-8. Epub 2004 Apr 1. PMID:15057273<ref>PMID:15057273</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1sez" style="background-color:#fffaf0;"></div>

[[Category: American tobacco]]

[[Category: Protoporphyrinogen oxidase]]

[[Category: Breithaupt, C]]

[[Category: Freigang, J]]

[[Category: Huber, R]]

[[Category: Kiefersauer, R]]

[[Category: Koch, M]]

[[Category: Messerschmidt, A]]

[[Category: Oxidoreductase]]