3jr3

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{{Seed}}
 
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[[Image:3jr3.jpg|left|200px]]
 
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{{STRUCTURE_3jr3| PDB=3jr3 | SCENE= }}
{{STRUCTURE_3jr3| PDB=3jr3 | SCENE= }}
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===Sir2 bound to acetylated peptide===
===Sir2 bound to acetylated peptide===
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{{ABSTRACT_PUBMED_019801667}}
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==Function==
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[[http://www.uniprot.org/uniprot/NPD_THEMA NPD_THEMA]] NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Has also depropionylation activity in vitro. Also able to ADP-ribosylate peptide substrates with Arg or Lys in the +2 position. The role of this function in vivo is not clear.<ref>PMID:17684016</ref><ref>PMID:16905097</ref><ref>PMID:19801667</ref>
==About this Structure==
==About this Structure==
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3JR3 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JR3 OCA].
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[[3jr3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JR3 OCA].
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==Reference==
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<ref group="xtra">PMID:019801667</ref><references group="xtra"/><references/>
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Hawse, W F.]]
[[Category: Hawse, W F.]]
[[Category: Wolberger, C.]]
[[Category: Wolberger, C.]]
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[[Category: Cytoplasm]]
 
[[Category: Deacetylation]]
[[Category: Deacetylation]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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[[Category: Ribosylation]]
[[Category: Ribosylation]]
[[Category: Sir2]]
[[Category: Sir2]]
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[[Category: Zinc]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 30 09:32:15 2009''
 

Revision as of 09:20, 27 March 2013

Template:STRUCTURE 3jr3

Contents

Sir2 bound to acetylated peptide

Template:ABSTRACT PUBMED 019801667

Function

[NPD_THEMA] NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Has also depropionylation activity in vitro. Also able to ADP-ribosylate peptide substrates with Arg or Lys in the +2 position. The role of this function in vivo is not clear.[1][2][3]

About this Structure

3jr3 is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

  • Hawse WF, Wolberger C. Structure-based mechanism of ADP-ribosylation by sirtuins. J Biol Chem. 2009 Nov 27;284(48):33654-61. Epub 2009 Sep 30. PMID:19801667 doi:10.1074/jbc.M109.024521
  1. ↑ Garrity J, Gardner JG, Hawse W, Wolberger C, Escalante-Semerena JC. N-lysine propionylation controls the activity of propionyl-CoA synthetase. J Biol Chem. 2007 Oct 12;282(41):30239-45. Epub 2007 Aug 7. PMID:17684016 doi:10.1074/jbc.M704409200
  2. ↑ Hoff KG, Avalos JL, Sens K, Wolberger C. Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide. Structure. 2006 Aug;14(8):1231-40. PMID:16905097 doi:http://dx.doi.org/10.1016/j.str.2006.06.006
  3. ↑ Hawse WF, Wolberger C. Structure-based mechanism of ADP-ribosylation by sirtuins. J Biol Chem. 2009 Nov 27;284(48):33654-61. Epub 2009 Sep 30. PMID:19801667 doi:10.1074/jbc.M109.024521

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