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1gy0

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Revision as of 06:37, 3 January 2018

crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL FORM C (P3121)

Structural highlights

1gy0 is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1gxy, 1gxz
Activity:	NAD(+)--protein-arginine ADP-ribosyltransferase, with EC number 2.4.2.31
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 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.

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^[1]

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

References

↑ Mueller-Dieckmann C, Ritter H, Haag F, Koch-Nolte F, Schulz GE. Structure of the ecto-ADP-ribosyl transferase ART2.2 from rat. J Mol Biol. 2002 Sep 27;322(4):687-96. PMID:12270706

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/1gy0"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2; CRYSTAL FORM C (P3121)==
+==crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL FORM C (P3121)==
 <StructureSection load='1gy0' size='340' side='right' caption='[[1gy0]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gxy|1gxy]], [[1gxz|1gxz]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)--protein-arginine_ADP-ribosyltransferase NAD(+)--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] </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=1gy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gy0 OCA], [http://pdbe.org/1gy0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gy0 RCSB], [http://www.ebi.ac.uk/pdbsum/1gy0 PDBsum]</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=1gy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gy0 OCA], [http://pdbe.org/1gy0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gy0 RCSB], [http://www.ebi.ac.uk/pdbsum/1gy0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gy0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gy0_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gy/1gy0_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1gy0

From Proteopedia

Revision as of 06:37, 3 January 2018

crystal structure of the eucaryotic mono-ADP-ribosyltransferase ART2.2; CRYSTAL FORM C (P3121)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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