4zdy

<StructureSection load='4zdy' size='340' side='right' caption='[[4zdy]], [[Resolution|resolution]] 2.02&Aring;' scene=''>

<table><tr><td colspan='2'>[[4zdy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZDY FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1YN:2-[(2R)-BUTAN-2-YL]-4-{4-[4-(4-{[(2R,4S)-2-(2,4-DICHLOROPHENYL)-2-(1H-1,2,4-TRIAZOL-1-YLMETHYL)-1,3-DIOXOLAN-4-YL]METHOXY}PHENYL)PIPERAZIN-1-YL]PHENYL}-2,4-DIHYDRO-3H-1,2,4-TRIAZOL-3-ONE'>1YN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zdz|4zdz]], [[4ze0|4ze0]], [[4ze1|4ze1]], [[4ze2|4ze2]], [[4ze3|4ze3]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdy OCA], [http://pdbe.org/4zdy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zdy RCSB], [http://www.ebi.ac.uk/pdbsum/4zdy PDBsum]</span></td></tr>

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== Publication Abstract from PubMed ==

Bitopic integral membrane proteins with a single transmembrane helix play diverse roles in catalysis, cell signaling, and morphogenesis. Complete monospanning protein structures are needed to show how interaction between the transmembrane helix and catalytic domain might influence association with the membrane and function. We report crystal structures of full-length Saccharomyces cerevisiae lanosterol 14alpha-demethylase, a membrane monospanning cytochrome P450 of the CYP51 family that catalyzes the first postcyclization step in ergosterol biosynthesis and is inhibited by triazole drugs. The structures reveal a well-ordered N-terminal amphipathic helix preceding a putative transmembrane helix that would constrain the catalytic domain orientation to lie partly in the lipid bilayer. The structures locate the substrate lanosterol, identify putative substrate and product channels, and reveal constrained interactions with triazole antifungal drugs that are important for drug design and understanding drug resistance.

 

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== References ==

[[Category: Keniya, M V]]

[[Category: Monk, B C]]

[[Category: Sagatova, A]]

[[Category: Tyndall, J D.A]]

[[Category: Wilson, R K]]

[[Category: Cyp51]]

[[Category: Itraconazole]]

[[Category: Resistance mutation]]