6etf

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m (Protected "6etf" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6etf is ON HOLD
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==The Structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate==
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<StructureSection load='6etf' size='340' side='right' caption='[[6etf]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6etf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ETF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ETF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene></td></tr>
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<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=6etf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6etf OCA], [http://pdbe.org/6etf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6etf RCSB], [http://www.ebi.ac.uk/pdbsum/6etf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6etf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CNX1_ARATH CNX1_ARATH]] Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.<ref>PMID:15504727</ref> <ref>PMID:16636046</ref> <ref>PMID:12590921</ref> <ref>PMID:15306815</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The molybdenum cofactor (Moco) is a redox-active prosthetic group found in the active site of Moco-dependent enzymes, which are vitally important for life. Moco biosynthesis involves several enzymes that catalyze the subsequent conversion of GTP into cyclic pyranopterin monophosphate (cPMP), molybdopterin (MPT), adenylated MPT (MPT-AMP), and finally Moco. While the underlying principles of cPMP, MPT, and MPT-AMP formation are well understood, the molybdenum insertase (Mo-insertase)-catalyzed final Moco maturation step is not. In the present study, we analyzed high-resolution X-ray datasets of the plant Mo-insertase Cnx1E that revealed two molybdate-binding sites within the active site, hence improving the current view on Cnx1E functionality. The presence of molybdate anions in either of these sites is tied to a distinctive backbone conformation, which we suggest to be essential for Mo-insertase molybdate selectivity and insertion efficiency.
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Authors: Krausze, J.
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The functional principle of eukaryotic molybdenum insertases.,Krausze J, Hercher TW, Zwerschke D, Kirk ML, Blankenfeldt W, Mendel RR, Kruse T Biochem J. 2018 May 24;475(10):1739-1753. doi: 10.1042/BCJ20170935. PMID:29717023<ref>PMID:29717023</ref>
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Description: The Structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6etf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Krausze, J]]
[[Category: Krausze, J]]
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[[Category: Adenosine monophosphate]]
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[[Category: Alternate binding]]
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[[Category: Arabidopsis]]
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[[Category: Arabidopsis protein]]
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[[Category: Catalytic domain]]
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[[Category: Coenzyme]]
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[[Category: Entropic enzyme]]
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[[Category: Insertion mechanism]]
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[[Category: Metalloprotein]]
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[[Category: Molybdate]]
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[[Category: Nucleotide binding]]
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[[Category: Plant protein]]

Revision as of 07:40, 18 July 2018

The Structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate

6etf, resolution 1.78Å

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