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| | ==Crystal structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana== | | ==Crystal structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana== |
| - | <StructureSection load='5g2r' size='340' side='right' caption='[[5g2r]], [[Resolution|resolution]] 2.45Å' scene=''> | + | <StructureSection load='5g2r' size='340' side='right'caption='[[5g2r]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5g2r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G2R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G2R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5g2r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G2R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g2s|5g2s]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Molybdopterin_molybdotransferase Molybdopterin molybdotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.10.1.1 2.10.1.1] </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=5g2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g2r OCA], [https://pdbe.org/5g2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g2r RCSB], [https://www.ebi.ac.uk/pdbsum/5g2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g2r ProSAT]</span></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=5g2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g2r OCA], [http://pdbe.org/5g2r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g2r RCSB], [http://www.ebi.ac.uk/pdbsum/5g2r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g2r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Molybdopterin molybdotransferase]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Heinz, D W]] | + | [[Category: Large Structures]] |
| - | [[Category: Krausze, J]] | + | [[Category: Heinz DW]] |
| - | [[Category: Kruse, T]] | + | [[Category: Krausze J]] |
| - | [[Category: Mendel, R R]] | + | [[Category: Kruse T]] |
| - | [[Category: Probst, C]] | + | [[Category: Mendel RR]] |
| - | [[Category: Saha, S]] | + | [[Category: Probst C]] |
| - | [[Category: Cnx1]]
| + | [[Category: Saha S]] |
| - | [[Category: Cnx1e]]
| + | |
| - | [[Category: Gephe]]
| + | |
| - | [[Category: Gephyrin]]
| + | |
| - | [[Category: Mo-insertase]]
| + | |
| - | [[Category: Moco]]
| + | |
| - | [[Category: Moea]]
| + | |
| - | [[Category: Molybdenum cofactor]]
| + | |
| - | [[Category: Molybdenum metabolism]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
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.[1] [2] [3] [4]
Publication Abstract from PubMed
The molybdenum cofactor (Moco) is a redox active prosthetic group, essentially required for numerous enzyme-catalyzed two electron transfer reactions. Moco is synthesized by an evolutionarily old and highly conserved multistep pathway. In the last step of Moco biosynthesis, the molybdenum center is inserted into the final Moco precursor adenylated molybdopterin (MPT-AMP). This unique and yet poorly characterized maturation reaction finally yields physiologically active Moco. In the model plant Arabidopsis, the two domain enzyme, Cnx1, is required for Moco formation. Recently, a genetic screen identified novel Arabidopsis cnx1 mutant plant lines each harboring a single amino acid exchange in the N-terminal Cnx1E domain. Biochemical characterization of the respective recombinant Cnx1E variants revealed two different amino acid exchanges (S197F and G175D) that impair Cnx1E dimerization, thus linking Cnx1E oligomerization to Cnx1 functionality. Analysis of the Cnx1E structure identified Cnx1E active site-bound molybdate and magnesium ions, which allowed to fine-map the Cnx1E MPT-AMP-binding site.
Dimerization of the plant molybdenum insertase Cnx1E is required for synthesis of the molybdenum cofactor.,Krausze J, Probst C, Curth U, Reichelt J, Saha S, Schafflick D, Heinz DW, Mendel RR, Kruse T Biochem J. 2017 Jan 1;474(1):163-178. doi: 10.1042/BCJ20160846. Epub 2016 Nov 1. PMID:27803248[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Llamas A, Mendel RR, Schwarz G. Synthesis of adenylated molybdopterin: an essential step for molybdenum insertion. J Biol Chem. 2004 Dec 31;279(53):55241-6. Epub 2004 Oct 25. PMID:15504727 doi:http://dx.doi.org/10.1074/jbc.M409862200
- ↑ Llamas A, Otte T, Multhaup G, Mendel RR, Schwarz G. The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly. J Biol Chem. 2006 Jul 7;281(27):18343-50. Epub 2006 Apr 24. PMID:16636046 doi:http://dx.doi.org/10.1074/jbc.M601415200
- ↑ Kuper J, Winking J, Hecht HJ, Mendel RR, Schwarz G. The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G. Arch Biochem Biophys. 2003 Mar 1;411(1):36-46. PMID:12590921
- ↑ Kuper J, Llamas A, Hecht HJ, Mendel RR, Schwarz G. Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolism. Nature. 2004 Aug 12;430(7001):803-6. PMID:15306815 doi:10.1038/nature02681
- ↑ Krausze J, Probst C, Curth U, Reichelt J, Saha S, Schafflick D, Heinz DW, Mendel RR, Kruse T. Dimerization of the plant molybdenum insertase Cnx1E is required for synthesis of the molybdenum cofactor. Biochem J. 2017 Jan 1;474(1):163-178. doi: 10.1042/BCJ20160846. Epub 2016 Nov 1. PMID:27803248 doi:http://dx.doi.org/10.1042/BCJ20160846
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