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5yfb

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Crystal structure of a new DPP III family member

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Retrieved from "http://52.214.119.220/wiki/index.php/5yfb"

Categories: Armillaria tabescens | Large Structures | Liu J | Sun Z | Xu T

@@ Line 3: / Line 3: @@
 <StructureSection load='5yfb' size='340' side='right'caption='[[5yfb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5yfb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YFB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YFB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5yfb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Armillaria_tabescens Armillaria tabescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YFB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.2&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dipeptidyl-peptidase_III Dipeptidyl-peptidase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.4 3.4.14.4] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5yfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yfb OCA], [http://pdbe.org/5yfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yfb RCSB], [http://www.ebi.ac.uk/pdbsum/5yfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yfb 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=5yfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yfb OCA], [https://pdbe.org/5yfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yfb RCSB], [https://www.ebi.ac.uk/pdbsum/5yfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yfb ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/B0S4Q0_ARMTA B0S4Q0_ARMTA]
-Aflatoxin-oxidase (AFO), a newly discovered oxidase isolated from Armillariella tabescens, was reported to perform aflatoxin B1 (AFB1) detoxification through breaking the bisfuran ring of AFB1. However, based on sequence alignment, we found that AFO shares high sequence identities with dipeptidyl peptidase III (DPP III) family members. To understand the functions of AFO, we determined its crystal structures in the absence and presence of zinc, copper ion, and employed HPLC to test if AFO could cleave the substrates of DPP III. Our structures reveal that AFO contains the classic DPP III activity center and the HPLC results further confirm that AFO possesses the dipeptidyl peptidase activity. Therefore, AFO should belong to DPP III family. Interestingly, unlike reported classic DPP III structure that has a large domain movement upon substrate binding, the AFO structures all adopt the closed conformation, independent of substrate binding. This conformation characteristic of AFO may be related to its enzyme activities. Taken together, our results demonstrate that AFO is a dual activity enzyme with both aflatoxin-oxidase and dipeptidyl peptidase activities and its unique conformation feature expands our understanding on the mode of reaction for this enzyme family.
-Crystal structures of Aflatoxin-oxidase from Armillariella tabescens reveal a dual activity enzyme.,Xu T, Xie C, Yao D, Zhou CZ, Liu J Biochem Biophys Res Commun. 2017 Dec 16;494(3-4):621-625. doi:, 10.1016/j.bbrc.2017.10.077. Epub 2017 Oct 16. PMID:29050944<ref>PMID:29050944</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5yfb" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Dipeptidyl peptidase 3D structures|Dipeptidyl peptidase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Dipeptidyl-peptidase III]]
+[[Category: Armillaria tabescens]]
 [[Category: Large Structures]]
-[[Category: Liu, J]]
+[[Category: Liu J]]
-[[Category: Sun, Z]]
+[[Category: Sun Z]]
-[[Category: Xu, T]]
+[[Category: Xu T]]
-[[Category: Aflatoxin-oxidase]]
-[[Category: Dipeptidyl peptidase iii]]
-[[Category: Hydrolase]]

5yfb

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Crystal structure of a new DPP III family member

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