1og3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1og3" [edit=sysop:move=sysop])
Current revision (07:32, 23 October 2024) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1og3.png|left|200px]]
 
-
{{STRUCTURE_1og3| PDB=1og3 | SCENE= }}
+
==Crystal structure of the eukaryotic mono-ADP-ribosyltransferase ART2.2 mutant E189I in complex with NAD==
 +
<StructureSection load='1og3' size='340' side='right'caption='[[1og3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1og3]] is a 1 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=1OG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OG3 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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=1og3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1og3 OCA], [https://pdbe.org/1og3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1og3 RCSB], [https://www.ebi.ac.uk/pdbsum/1og3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1og3 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/NAR2B_RAT NAR2B_RAT] Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity (to a lesser extent).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/og/1og3_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1og3 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The structures of beta-methylenethiazole-4-carboxamide adenine dinucleotide (TAD), NAD(+), and NADH as bound to ecto-ADP-ribosyltransferase 2.2 from rat and to its mutants E189I and E189A, respectively, have been established. The positions and conformations of NAD(+) and its analogues agree in general with those in other ADP-ribosyltransferases. The kinetic constants for NAD(+) hydrolysis were determined by RP-HPLC. The specific activity amounts to 26 units/mg, which is 6000-fold higher than a previously reported rate and 500-fold higher than the hydrolysis rates of other ADP-ribosyltransferases, confirming that hydrolysis is the major function of this enzyme. On the basis of structures and mutant activities, a catalytic mechanism is proposed. The known auto-ADP-ribosylation of the enzyme at the suggested position R184 is supported by one of the crystal structures where the nucleophile position is occupied by an Neta atom of this arginine which in turn is backed up by the base E159.
-
===CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2 MUTANT E189I IN COMPLEX WITH NAD===
+
Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat.,Ritter H, Koch-Nolte F, Marquez VE, Schulz GE Biochemistry. 2003 Sep 2;42(34):10155-62. PMID:12939142<ref>PMID:12939142</ref>
-
{{ABSTRACT_PUBMED_12939142}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 1og3" style="background-color:#fffaf0;"></div>
-
[[1og3]] is a 1 chain structure with 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=1OG3 OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:012939142</ref><references group="xtra"/>
+
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
-
[[Category: Koch-Nolte, F.]]
+
[[Category: Koch-Nolte F]]
-
[[Category: Marquez, V E.]]
+
[[Category: Marquez VE]]
-
[[Category: Ritter, H.]]
+
[[Category: Ritter H]]
-
[[Category: Schulz, G E.]]
+
[[Category: Schulz GE]]
-
[[Category: Adp-ribosyltransferase]]
+
-
[[Category: Immuno-regulation]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of the eukaryotic mono-ADP-ribosyltransferase ART2.2 mutant E189I in complex with NAD

PDB ID 1og3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1og3"
Personal tools