6etf: Difference between revisions

Latest revision as of 09:15, 11 November 2020

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

Structural highlights

6etf is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	AMP, EDO, MG, MOO
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

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^[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:https://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:https://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, Hercher TW, Zwerschke D, Kirk ML, Blankenfeldt W, Mendel RR, Kruse T. The functional principle of eukaryotic molybdenum insertases. Biochem J. 2018 May 24;475(10):1739-1753. doi: 10.1042/BCJ20170935. PMID:29717023 doi:https://dx.doi.org/10.1042/BCJ20170935

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1074/jbc.M409862200

[2] 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:https://dx.doi.org/10.1074/jbc.M601415200

[3] 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

[4] 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

[5] Krausze J, Hercher TW, Zwerschke D, Kirk ML, Blankenfeldt W, Mendel RR, Kruse T. The functional principle of eukaryotic molybdenum insertases. Biochem J. 2018 May 24;475(10):1739-1753. doi: 10.1042/BCJ20170935. PMID:29717023 doi:https://dx.doi.org/10.1042/BCJ20170935

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@@ Line 1: / Line 1: @@
 ==The Structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate==
-<StructureSection load='6etf' size='340' side='right' caption='[[6etf]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
+<StructureSection load='6etf' size='340' side='right'caption='[[6etf]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<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://proteopedia.org/fgij/fg.htm?mol=6ETF 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>
+</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=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='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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
 </table>
 == Function ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Krausze, J]]
 [[Category: Adenosine monophosphate]]

6etf: Difference between revisions

Latest revision as of 09:15, 11 November 2020

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

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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