6eth: 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 tungstate

Structural highlights

6eth is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ACE, AMP, EDO, MG, WO4
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

[1]

[2]

[3]

[4]

[5]

@@ Line 1: / Line 1: @@
 ==The Structure of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and tungstate==
-<StructureSection load='6eth' size='340' side='right' caption='[[6eth]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
+<StructureSection load='6eth' size='340' side='right'caption='[[6eth]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6eth]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ETH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ETH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6eth]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ETH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ETH FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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=WO4:TUNGSTATE(VI)ION'>WO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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=WO4:TUNGSTATE(VI)ION'>WO4</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=6eth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eth OCA], [http://pdbe.org/6eth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eth RCSB], [http://www.ebi.ac.uk/pdbsum/6eth PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eth 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=6eth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eth OCA], [http://pdbe.org/6eth PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eth RCSB], [http://www.ebi.ac.uk/pdbsum/6eth PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eth ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Krausze, J]]
 [[Category: Adenosine monophosphate]]

6eth: 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 tungstate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools