6gbc: Difference between revisions

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'''Unreleased structure'''


The entry 6gbc is ON HOLD until Paper Publication
==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]] 1.59&Aring;' 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.


Authors: Krausze, J.
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>


Description: The Structure of variant R369A of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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]]

Latest revision as of 10:43, 18 July 2018

The Structure of variant R369A of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdateThe Structure of variant R369A of the Mo-insertase domain Cnx1E from Arabidopsis thaliana in complex with AMP and molybdate

Structural highlights

6gbc is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:
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

  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:http://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:http://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:http://dx.doi.org/10.1042/BCJ20170935

6gbc, resolution 1.59Å

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