5oel

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Current revision (16:46, 13 December 2023) (edit) (undo)
 
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<StructureSection load='5oel' size='340' side='right'caption='[[5oel]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5oel' size='340' side='right'caption='[[5oel]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5oel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OEL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OEL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5oel]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_CDC1551 Mycobacterium tuberculosis CDC1551]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OEL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1W6:ETHYL+({2-[(1,3-BENZOTHIAZOL-2-YLCARBONYL)AMINO]THIOPHEN-3-YL}CARBONYL)CARBAMATE'>1W6</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kw5|4kw5]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1W6:ETHYL+({2-[(1,3-BENZOTHIAZOL-2-YLCARBONYL)AMINO]THIOPHEN-3-YL}CARBONYL)CARBAMATE'>1W6</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Decaprenylphospho-beta-D-ribofuranose_2-oxidase Decaprenylphospho-beta-D-ribofuranose 2-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.98.3 1.1.98.3] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oel OCA], [https://pdbe.org/5oel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oel RCSB], [https://www.ebi.ac.uk/pdbsum/5oel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oel ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5oel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oel OCA], [http://pdbe.org/5oel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oel RCSB], [http://www.ebi.ac.uk/pdbsum/5oel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oel ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DPRE1_MYCTO DPRE1_MYCTO]] Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans. DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex. Can also use farnesyl-phosphoryl-beta-D-ribofuranose (FPR) as substrate in vitro.[UniProtKB:P9WJF1] DprE1 is a highly vulnerable and fully validated tuberculosis drug target.[UniProtKB:P9WJF1]
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[https://www.uniprot.org/uniprot/DPRE1_MYCTU DPRE1_MYCTU] Involved in the epimerization of decaprenylphosphoryl ribose (DPR) to decaprenylphosphoryl arabinose (DPA) a precursor for arabinan synthesis in mycobacterial cell wall biosynthesis. Probably catalyzes the oxidation at C-2 of decaprenylphosphoryl ribose (DPR) to yield decaprenylphosphoryl 2-keto-ribose (DPX).<ref>PMID:16291675</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Decaprenylphospho-beta-D-ribofuranose 2-oxidase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Batt, S M]]
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[[Category: Mycobacterium tuberculosis CDC1551]]
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[[Category: Besra, G S]]
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[[Category: Batt SM]]
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[[Category: Futterer, K]]
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[[Category: Besra GS]]
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[[Category: Fad-containing oxidoreductase decaprenylphosphoarabinose synthesis]]
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[[Category: Futterer K]]
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[[Category: Oxidoreductase]]
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Current revision

Mycobacterium tuberculosis DprE1 mutant Y314C in complex with TCA1

PDB ID 5oel

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