1gxz

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[[Image:1gxz.gif|left|200px]]
 
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{{Structure
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==crystal structure of the eukaryotic mono-ADP-ribosyltransferase ART2.2; Crystal form B (P212121)==
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|PDB= 1gxz |SIZE=350|CAPTION= <scene name='initialview01'>1gxz</scene>, resolution 2.1&Aring;
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<StructureSection load='1gxz' size='340' side='right'caption='[[1gxz]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Brt+Binding+Site+For+Chain+B'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BRT:5-BROMONICOTINAMIDE'>BRT</scene>
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<table><tr><td colspan='2'>[[1gxz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXZ FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(P)(+)--protein-arginine_ADP-ribosyltransferase NAD(P)(+)--protein-arginine ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.31 2.4.2.31]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRT:5-BROMONICOTINAMIDE'>BRT</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxz OCA], [https://pdbe.org/1gxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxz RCSB], [https://www.ebi.ac.uk/pdbsum/1gxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxz ProSAT]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2; CRYSTAL FORM B (P212121)'''
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== Function ==
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[https://www.uniprot.org/uniprot/NAR2B_RAT NAR2B_RAT] Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity (to a lesser extent).
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== Evolutionary Conservation ==
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==Overview==
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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/gx/1gxz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1gxz 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 ==
The mammalian extracellular ADP-ribosyl transferases ART1 through ART5 are sequence-related to each other. Among them ART2 is involved in immuno regulation. The variant ART2.2 was expressed in the periplasm of Escherichia coli and crystallized. Its structure was determined by X-ray diffraction at 1.7A resolution in one crystal form and at slightly lower resolutions in two others. The active center was indicated by a ligated nicotinamide analogue, which also revealed a small induced-fit. The centerpiece of the chainfold of ART2.2 agrees with those of all bacterial ADP-ribosyl transferases. This correspondence and the nicotinamide position were used to model the binding structure of the whole substrate NAD(+) at ART2.2. Two of the bacterial enzymes are structurally more closely related to ART2.2 while the others are more closely related to the eukaryotic poly(ADP-ribosyl)polymerase. This splits the ADP-ribosyl transferases into two distinct subfamilies. A special feature of ART2.2 is its long N-terminal extension and two disulfide bridges that are far away from the active center. They stabilize the protein against denaturation and presumably also against shearing forces parallel with the membrane where ART2.2 is anchored.
The mammalian extracellular ADP-ribosyl transferases ART1 through ART5 are sequence-related to each other. Among them ART2 is involved in immuno regulation. The variant ART2.2 was expressed in the periplasm of Escherichia coli and crystallized. Its structure was determined by X-ray diffraction at 1.7A resolution in one crystal form and at slightly lower resolutions in two others. The active center was indicated by a ligated nicotinamide analogue, which also revealed a small induced-fit. The centerpiece of the chainfold of ART2.2 agrees with those of all bacterial ADP-ribosyl transferases. This correspondence and the nicotinamide position were used to model the binding structure of the whole substrate NAD(+) at ART2.2. Two of the bacterial enzymes are structurally more closely related to ART2.2 while the others are more closely related to the eukaryotic poly(ADP-ribosyl)polymerase. This splits the ADP-ribosyl transferases into two distinct subfamilies. A special feature of ART2.2 is its long N-terminal extension and two disulfide bridges that are far away from the active center. They stabilize the protein against denaturation and presumably also against shearing forces parallel with the membrane where ART2.2 is anchored.
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==About this Structure==
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Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat.,Mueller-Dieckmann C, Ritter H, Haag F, Koch-Nolte F, Schulz GE J Mol Biol. 2002 Sep 27;322(4):687-96. PMID:12270706<ref>PMID:12270706</ref>
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1GXZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXZ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat., Mueller-Dieckmann C, Ritter H, Haag F, Koch-Nolte F, Schulz GE, J Mol Biol. 2002 Sep 27;322(4):687-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12270706 12270706]
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</div>
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[[Category: NAD(P)(+)--protein-arginine ADP-ribosyltransferase]]
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<div class="pdbe-citations 1gxz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Mueller-Dieckmann C]]
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[[Category: Mueller-Dieckmann, C.]]
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[[Category: Schulz GE]]
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[[Category: Schulz, G E.]]
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[[Category: BRT]]
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[[Category: adp-ribosyltransferase]]
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[[Category: immuno-regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:29:29 2008''
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Current revision

crystal structure of the eukaryotic mono-ADP-ribosyltransferase ART2.2; Crystal form B (P212121)

PDB ID 1gxz

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