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2lgr

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Revision as of 19:49, 1 August 2018

Solution structure of human protein C6orf130, a putative macro domain

Structural highlights

2lgr is a 1 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 2jyc. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2l8r
Gene:	BC011709.2, C6orf130 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OARD1_HUMAN] Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.

Publication Abstract from PubMed

Post-translational modification of proteins/histones by lysine acylation has profound effects on the physiological function of modified proteins. Deacylation by NAD(+)-dependent sirtuin reactions yields as a product O-acyl-ADP-ribose, which has been implicated as a signaling molecule in modulating cellular processes. Macrodomain-containing proteins are reported to bind NAD(+)-derived metabolites. Here, we describe the structure and function of an orphan macrodomain protein, human C6orf130. This unique 17-kDa protein is a stand-alone macrodomain protein that occupies a distinct branch in the phylogenic tree. We demonstrate that C6orf130 catalyzes the efficient deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose, and O-butyryl-ADP-ribose to produce ADP-ribose (ADPr) and acetate, propionate, and butyrate, respectively. Using NMR spectroscopy, we solved the structure of C6orf130 in the presence and absence of ADPr. The structures showed a canonical fold with a deep ligand (ADPr)-binding cleft. Structural comparisons of apo-C6orf130 and the ADPr-C6orf130 complex revealed fluctuations of the beta(5)-alpha(4) loop that covers the bound ADPr, suggesting that the beta(5)-alpha(4) loop functions as a gate to sequester substrate and offer flexibility to accommodate alternative substrates. The ADPr-C6orf130 complex identified amino acid residues involved in substrate binding and suggested residues that function in catalysis. Site-specific mutagenesis and steady-state kinetic analyses revealed two critical catalytic residues, Ser-35 and Asp-125. We propose a catalytic mechanism for deacylation of O-acyl-ADP-ribose by C6orf130 and discuss the biological implications in the context of reversible protein acylation at lysine residues.

Orphan Macrodomain Protein (Human C6orf130) Is an O-Acyl-ADP-ribose Deacylase: SOLUTION STRUCTURE AND CATALYTIC PROPERTIES.,Peterson FC, Chen D, Lytle BL, Rossi MN, Ahel I, Denu JM, Volkman BF J Biol Chem. 2011 Oct 14;286(41):35955-65. Epub 2011 Aug 17. PMID:21849506^[1]

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

References

↑ Peterson FC, Chen D, Lytle BL, Rossi MN, Ahel I, Denu JM, Volkman BF. Orphan Macrodomain Protein (Human C6orf130) Is an O-Acyl-ADP-ribose Deacylase: SOLUTION STRUCTURE AND CATALYTIC PROPERTIES. J Biol Chem. 2011 Oct 14;286(41):35955-65. Epub 2011 Aug 17. PMID:21849506 doi:10.1074/jbc.M111.276238

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2lgr"

@@ Line 1: / Line 1: @@
 ==Solution structure of human protein C6orf130, a putative macro domain==
 <StructureSection load='2lgr' size='340' side='right' caption='[[2lgr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2l8r|2l8r]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC011709.2, C6orf130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2lgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgr OCA], [http://pdbe.org/2lgr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lgr RCSB], [http://www.ebi.ac.uk/pdbsum/2lgr 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=2lgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgr OCA], [http://pdbe.org/2lgr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lgr RCSB], [http://www.ebi.ac.uk/pdbsum/2lgr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgr ProSAT]</span></td></tr>
 </table>
 == Function ==

2lgr

From Proteopedia

Revision as of 19:49, 1 August 2018

Solution structure of human protein C6orf130, a putative macro domain

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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