3g9d

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[[Image:3g9d.png|left|200px]]
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==Crystal structure glycohydrolase==
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<StructureSection load='3g9d' size='340' side='right' caption='[[3g9d]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3g9d]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G9D FirstGlance]. <br>
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</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>
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<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 Azospirillum brasilense])</td></tr>
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<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>
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<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://www.rcsb.org/pdb/explore.do?structureId=3g9d RCSB], [http://www.ebi.ac.uk/pdbsum/3g9d PDBsum]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g9/3g9d_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_3g9d| PDB=3g9d | SCENE= }}
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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<ref>PMID:19477184</ref>
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===Crystal structure glycohydrolase===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_19477184}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[3g9d]] is a 2 chain structure with sequence from [http://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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:019477184</ref><references group="xtra"/>
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[[Category: Azospirillum brasilense]]
[[Category: Azospirillum brasilense]]
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[[Category: Li, X D.]]
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[[Category: Li, X D]]
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[[Category: Winkler, F K.]]
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[[Category: Winkler, F K]]
[[Category: Adp-ribosylation]]
[[Category: Adp-ribosylation]]
[[Category: Drag]]
[[Category: Drag]]

Revision as of 10:06, 3 December 2014

Crystal structure glycohydrolase

3g9d, resolution 2.50Å

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