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1og4

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Crystal Structure of the Eucaryotic Mono-ADP-Ribosyltransferase ART2.2 Mutant E189A in Complex with NADH

Structural highlights

1og4 is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NAR2B_RAT Has both NAD(+) glycohydrolase and ADP-ribosyltransferase activity (to a lesser extent).

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

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ritter H, Koch-Nolte F, Marquez VE, Schulz GE. Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat. Biochemistry. 2003 Sep 2;42(34):10155-62. PMID:12939142 doi:http://dx.doi.org/10.1021/bi034625w

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1og4"

@@ Line 3: / Line 3: @@
 <StructureSection load='1og4' size='340' side='right'caption='[[1og4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1og4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OG4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1og4]] 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=1OG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OG4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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]] 2.6&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gxy|1gxy]], [[1gxz|1gxz]], [[1gy0|1gy0]], [[1og1|1og1]], [[1og3|1og3]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(+)--protein-arginine_ADP-ribosyltransferase NAD(+)--protein-arginine ADP-ribosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.31 2.4.2.31] </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=1og4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1og4 OCA], [https://pdbe.org/1og4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1og4 RCSB], [https://www.ebi.ac.uk/pdbsum/1og4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1og4 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).
+[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]]
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Koch-Nolte, F]]
+[[Category: Rattus norvegicus]]
-[[Category: Marquez, V E]]
+[[Category: Koch-Nolte F]]
-[[Category: Ritter, H]]
+[[Category: Marquez VE]]
-[[Category: Schulz, G E]]
+[[Category: Ritter H]]
-[[Category: Adp-ribosyltransferase]]
+[[Category: Schulz GE]]
-[[Category: Immuno-regulation]]
-[[Category: Transferase]]

1og4

From Proteopedia

Current revision

Crystal Structure of the Eucaryotic Mono-ADP-Ribosyltransferase ART2.2 Mutant E189A in Complex with NADH

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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