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| | <StructureSection load='6rms' size='340' side='right'caption='[[6rms]], [[Resolution|resolution]] 1.74Å' scene=''> | | <StructureSection load='6rms' size='340' side='right'caption='[[6rms]], [[Resolution|resolution]] 1.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rms]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RMS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RMS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rms]] 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=6RMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RMS 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=IMD:IMIDAZOLE'>IMD</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">Hybrid , X-ray diffraction , X-ray solution scattering, [[Resolution|Resolution]] 1.74Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rms OCA], [http://pdbe.org/6rms PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rms RCSB], [http://www.ebi.ac.uk/pdbsum/6rms PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rms 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=6rms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rms OCA], [https://pdbe.org/6rms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rms RCSB], [https://www.ebi.ac.uk/pdbsum/6rms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rms 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: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Krausze, J]] | + | [[Category: Krausze J]] |
| - | [[Category: Adenosine monophosphate]]
| + | |
| - | [[Category: Arabidopsis]]
| + | |
| - | [[Category: Arabidopsis protein]]
| + | |
| - | [[Category: Catalytic domain]]
| + | |
| - | [[Category: Metalloprotein]]
| + | |
| - | [[Category: Nucleotide binding]]
| + | |
| - | [[Category: Plant protein]]
| + | |
| Structural highlights
6rms is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | Hybrid , X-ray diffraction , X-ray solution scattering, Resolution 1.74Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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
Molybdenum insertases (Mo-insertases) catalyze the final step of molybdenum cofactor (Moco) biosynthesis, an evolutionary old and highly conserved multi-step pathway. In the first step of the pathway, GTP serves as substrate for the formation of cyclic pyranopterin monophosphate, which is subsequently converted into molybdopterin (MPT) in the second pathway step. In the following synthesis steps, MPT is adenylated yielding MPT-AMP that is subsequently used as substrate for enzyme catalyzed molybdate insertion. Molybdate insertion and MPT-AMP hydrolysis are catalyzed by the Mo-insertase E-domain. Earlier work reported a highly conserved aspartate residue to be essential for Mo-insertase functionality. In this work, we confirmed the mechanistic relevance of this residue for the Arabidopsis thaliana Mo-insertase Cnx1E. We found that the conservative substitution of Cnx1E residue Asp274 by Glu (D274E) leads to an arrest of MPT-AMP hydrolysis and hence to the accumulation of MPT-AMP. We further showed that the MPT-AMP accumulation goes in hand with the accumulation of molybdate. By crystallization and structure determination of the Cnx1E variant D274E, we identified the potential reason for the missing hydrolysis activity in the disorder of the region spanning amino acids 269 to 274. We reasoned that this is caused by the inability of a glutamate in position 274 to coordinate the octahedral Mg2+-water complex in the Cnx1E active site.
Insights into the Cnx1E catalyzed MPT-AMP hydrolysis.,Hercher TW, Krausze J, Hoffmeister S, Zwerschke D, Lindel T, Blankenfeldt W, Mendel RR, Kruse T Biosci Rep. 2020 Jan 31;40(1). pii: 221653. doi: 10.1042/BSR20191806. PMID:31860061[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
- ↑ Hercher TW, Krausze J, Hoffmeister S, Zwerschke D, Lindel T, Blankenfeldt W, Mendel RR, Kruse T. Insights into the Cnx1E catalyzed MPT-AMP hydrolysis. Biosci Rep. 2020 Jan 31;40(1). pii: 221653. doi: 10.1042/BSR20191806. PMID:31860061 doi:http://dx.doi.org/10.1042/BSR20191806
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