6gbc
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6gbc is ON HOLD until Paper Publication Authors: Krausze, J. Description: The Structure of variant R369A of the Mo-insertase domain Cnx1E from Arab...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The Structure of variant R369A of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate== |
| + | <StructureSection load='6gbc' size='340' side='right' caption='[[6gbc]], [[Resolution|resolution]] 1.59Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6gbc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GBC FirstGlance]. <br> | ||
| + | </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> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></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=6gbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gbc OCA], [http://pdbe.org/6gbc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gbc RCSB], [http://www.ebi.ac.uk/pdbsum/6gbc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gbc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 6gbc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Krausze, J]] | [[Category: Krausze, J]] | ||
| + | [[Category: Adenosine monophosphate]] | ||
| + | [[Category: Arabidopsis]] | ||
| + | [[Category: Arabidopsis protein]] | ||
| + | [[Category: Catalytic domain]] | ||
| + | [[Category: Coenzyme]] | ||
| + | [[Category: Entropic enzyme]] | ||
| + | [[Category: Metalloprotein]] | ||
| + | [[Category: Nucleotide binding]] | ||
| + | [[Category: Transferase]] | ||
Current revision
The Structure of variant R369A of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate
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