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| | ==Crystal structure glycohydrolase== | | ==Crystal structure glycohydrolase== |
| - | <StructureSection load='3g9d' size='340' side='right' caption='[[3g9d]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3g9d' size='340' side='right'caption='[[3g9d]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g9d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29145 Atcc 29145]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G9D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g9d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azospirillum_brasilense Azospirillum brasilense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G9D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">draG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192 ATCC 29145])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ADP-ribosyl-[dinitrogen_reductase]_hydrolase ADP-ribosyl-[dinitrogen reductase] hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.24 3.2.2.24] </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=3g9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9d OCA], [https://pdbe.org/3g9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g9d RCSB], [https://www.ebi.ac.uk/pdbsum/3g9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9d 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=3g9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g9d OCA], [http://pdbe.org/3g9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g9d RCSB], [http://www.ebi.ac.uk/pdbsum/3g9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g9d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A7XNI2_AZOBR A7XNI2_AZOBR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 29145]] | + | [[Category: Azospirillum brasilense]] |
| - | [[Category: Li, X D]] | + | [[Category: Large Structures]] |
| - | [[Category: Winkler, F K]] | + | [[Category: Li X-D]] |
| - | [[Category: Adp-ribosylation]]
| + | [[Category: Winkler FK]] |
| - | [[Category: Drag]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nitrogenase]]
| + | |
| - | [[Category: Posttranslational modification]]
| + | |
| Structural highlights
Function
A7XNI2_AZOBR
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Protein-reversible ADP-ribosylation is emerging as an important post-translational modification used to control enzymatic and protein activity in different biological systems. This modification regulates nitrogenase activity in several nitrogen-fixing bacterial species. ADP-ribosylation is catalyzed by ADP-ribosyltransferases and is reversed by ADP-ribosylhydrolases. The structure of the ADP-ribosylhydrolase that acts on Azospirillum brasilense nitrogenase (dinitrogenase reductase-activating glycohydrolase, DraG) has been solved at a resolution of 2.5 A. This bacterial member of the ADP-ribosylhydrolase family acts specifically towards a mono-ADP-ribosylated substrate. The protein shows an all-alpha-helix structure with two magnesium ions located in the active site. Comparison of the DraG structure with orthologues deposited in the Protein Data Bank from Archaea and mammals indicates that the ADP-ribosylhydrolase fold is conserved in all domains of life. Modeling of the binding of the substrate ADP-ribosyl moiety to DraG is in excellent agreement with biochemical data.
Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket.,Li XD, Huergo LF, Gasperina A, Pedrosa FO, Merrick M, Winkler FK J Mol Biol. 2009 Jul 24;390(4):737-46. Epub 2009 May 25. PMID:19477184[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li XD, Huergo LF, Gasperina A, Pedrosa FO, Merrick M, Winkler FK. Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket. J Mol Biol. 2009 Jul 24;390(4):737-46. Epub 2009 May 25. PMID:19477184 doi:10.1016/j.jmb.2009.05.031
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