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==Crystal structure of arabidopsis N6-mAMP deaminase MAPDA== | ==Crystal structure of arabidopsis N6-mAMP deaminase MAPDA== | ||
<StructureSection load='6iv5' size='340' side='right' caption='[[6iv5]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='6iv5' size='340' side='right'caption='[[6iv5]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6iv5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IV5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6iv5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IV5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At4g04880, T4B21.20, T4B21_20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=6iv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iv5 OCA], [http://pdbe.org/6iv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iv5 RCSB], [http://www.ebi.ac.uk/pdbsum/6iv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iv5 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=6iv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iv5 OCA], [http://pdbe.org/6iv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iv5 RCSB], [http://www.ebi.ac.uk/pdbsum/6iv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iv5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Arabidopsis thaliana aminohydrolase (AtADAL) has been shown to be involved in the metabolism of N(6)-methyl-AMP, a proposed intermediate during m(6)A-modified RNA metabolism, which can be subsequently incorporated into newly synthesized RNA by Pol II. It has been proposed that AtADAL will prevent N(6)-methyl-AMP reuse and catabolize it to inosine monophosphate (IMP). Here, we have solved the crystal structures of AtADAL in the apo form and in complex with GMP and IMP in the presence of Zn(2+). We have identified the substrate-binding pocket of AtADAL and compared it with that for adenosine deaminase (ADA), adenine deaminase (ADE) and AMP deaminase (AMPD) from multiple species. The comparisons reveal that plant ADAL1 may have the potential ability to catalyze different alkyl-group substituted substrates. | |||
Structure of Arabidopsis thaliana N(6)-methyl-AMP deaminase ADAL with bound GMP and IMP and implications for N(6)-methyl-AMP recognition and processing.,Wu B, Zhang D, Nie H, Shen S, Li Y, Li S RNA Biol. 2019 Jul 18:1-9. doi: 10.1080/15476286.2019.1642712. PMID:31318636<ref>PMID:31318636</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6iv5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | |||
[[Category: Large Structures]] | |||
[[Category: Li, S S]] | [[Category: Li, S S]] | ||
[[Category: Nie, H B]] | [[Category: Nie, H B]] | ||
Revision as of 09:55, 31 July 2019
Crystal structure of arabidopsis N6-mAMP deaminase MAPDACrystal structure of arabidopsis N6-mAMP deaminase MAPDA
Structural highlights
Publication Abstract from PubMedArabidopsis thaliana aminohydrolase (AtADAL) has been shown to be involved in the metabolism of N(6)-methyl-AMP, a proposed intermediate during m(6)A-modified RNA metabolism, which can be subsequently incorporated into newly synthesized RNA by Pol II. It has been proposed that AtADAL will prevent N(6)-methyl-AMP reuse and catabolize it to inosine monophosphate (IMP). Here, we have solved the crystal structures of AtADAL in the apo form and in complex with GMP and IMP in the presence of Zn(2+). We have identified the substrate-binding pocket of AtADAL and compared it with that for adenosine deaminase (ADA), adenine deaminase (ADE) and AMP deaminase (AMPD) from multiple species. The comparisons reveal that plant ADAL1 may have the potential ability to catalyze different alkyl-group substituted substrates. Structure of Arabidopsis thaliana N(6)-methyl-AMP deaminase ADAL with bound GMP and IMP and implications for N(6)-methyl-AMP recognition and processing.,Wu B, Zhang D, Nie H, Shen S, Li Y, Li S RNA Biol. 2019 Jul 18:1-9. doi: 10.1080/15476286.2019.1642712. PMID:31318636[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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