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4c8r

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Revision as of 17:32, 7 September 2022

Human gamma-butyrobetaine dioxygenase (BBOX1) in complex with Ni(II) and N-(3-hydroxypicolinoyl)-S-(pyridin-2-ylmethyl)-L-cysteine (AR692B)

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Retrieved from "http://52.214.119.220/wiki/index.php/4c8r"

@@ Line 3: / Line 3: @@
 <StructureSection load='4c8r' size='340' side='right'caption='[[4c8r]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4c8r]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4C8R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4c8r]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C8R FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6YT:N-(3-HYDROXYPICOLINOYL)-S-(PYRIDIN-2-YLMETHYL)-L-CYSTEINE'>6YT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gamma-butyrobetaine_dioxygenase Gamma-butyrobetaine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.1 1.14.11.1] </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=4c8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8r OCA], [https://pdbe.org/4c8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c8r RCSB], [https://www.ebi.ac.uk/pdbsum/4c8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c8r ProSAT]</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=4c8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c8r OCA], [http://pdbe.org/4c8r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c8r RCSB], [http://www.ebi.ac.uk/pdbsum/4c8r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c8r ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BODG_HUMAN BODG_HUMAN]] Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
+[[https://www.uniprot.org/uniprot/BODG_HUMAN BODG_HUMAN]] Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Carnitine is essential for fatty acid metabolism, but is associated with both health benefits and risks, especially heart diseases. We report the identification of potent, selective and cell active inhibitors of gamma-butyrobetaine hydroxylase (BBOX), which catalyses the final step of carnitine biosynthesis in animals. A crystal structure of BBOX in complex with a lead inhibitor reveals that it binds in two modes, one of which adopts an unusual 'U-shape' conformation stabilised by inter- and intra-molecular pi-stacking interactions. Conformational changes observed on binding of the inhibitor to BBOX likely reflect those occurring in catalysis; they also rationalise the inhibition of BBOX by high levels of its substrate gamma-butyrobetaine (GBB), as observed both with isolated BBOX protein and in cellular studies.
-Modulating carnitine levels by targeting its biosynthesis pathway - selective inhibition of gamma-butyrobetaine hydroxylase.,Rydzik AM, Chowdhury R, Kochan GT, Williams ST, McDonough MA, Kawamura A, Schofield CJ Chem Sci. 2014 May 1;5(5):1765-1771. doi: 10.1039/C4SC00020J. PMID:26682037<ref>PMID:26682037</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4c8r" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Gamma-butyrobetaine dioxygenase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Chowdhury, R]]
+[[Category: Chowdhury R]]
-[[Category: Kochan, G T]]
+[[Category: Kochan GT]]
-[[Category: McDonough, M A]]
+[[Category: McDonough MA]]
-[[Category: Rydzik, A M]]
+[[Category: Rydzik AM]]
-[[Category: Schofield, C J]]
+[[Category: Schofield CJ]]
-[[Category: 2-oxoglutarate]]
-[[Category: Dioxygenase 1]]
-[[Category: Dsbh]]
-[[Category: Facial triad]]
-[[Category: Gamma-butyrobetaine]]
-[[Category: Hydroxylase]]
-[[Category: Iron]]
-[[Category: Non-heme]]
-[[Category: Oxidoreductase]]

4c8r

From Proteopedia

Revision as of 17:32, 7 September 2022

Human gamma-butyrobetaine dioxygenase (BBOX1) in complex with Ni(II) and N-(3-hydroxypicolinoyl)-S-(pyridin-2-ylmethyl)-L-cysteine (AR692B)

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Function

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