2lgr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2lgr.png|left|200px]]
+
==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=''>
 +
== Structural highlights ==
 +
[[2lgr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jyc 2jyc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGR OCA]. <br>
 +
<b>Related:</b> [[2l8r|2l8r]]<br>
 +
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
 +
== 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<ref>PMID:21849506</ref>
-
The line below this paragraph, containing "STRUCTURE_2lgr", creates the "Structure Box" on the page.
+
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
-
or leave the SCENE parameter empty for the default display.
+
-
-->
+
-
{{STRUCTURE_2lgr| PDB=2lgr | SCENE= }}
+
-
===Solution structure of human protein C6orf130, a putative macro domain===
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
== References ==
-
 
+
<references/>
-
<!--
+
__TOC__
-
The line below this paragraph, {{ABSTRACT_PUBMED_21849506}}, adds the Publication Abstract to the page
+
</StructureSection>
-
(as it appears on PubMed at http://www.pubmed.gov), where 21849506 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_21849506}}
+
-
 
+
-
==About this Structure==
+
-
[[2lgr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2jyc 2jyc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGR OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:021849506</ref><references group="xtra"/>
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
[[Category: CESG, Center for Eukaryotic Structural Genomics.]]

Revision as of 08:27, 30 April 2014

Solution structure of human protein C6orf130, a putative macro domain

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/2lgr"
Personal tools