1yc5

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[[Image:1yc5.gif|left|200px]]<br /><applet load="1yc5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1yc5.gif|left|200px]]
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caption="1yc5, resolution 1.40&Aring;" />
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'''Sir2-p53 peptide-nicotinamide'''<br />
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{{Structure
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|PDB= 1yc5 |SIZE=350|CAPTION= <scene name='initialview01'>1yc5</scene>, resolution 1.40&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=NCA:NICOTINAMIDE'>NCA</scene>
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|ACTIVITY=
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|GENE= npdA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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}}
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'''Sir2-p53 peptide-nicotinamide'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1YC5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=NCA:'>NCA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YC5 OCA].
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1YC5 is a [[Protein complex]] 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=1YC5 OCA].
==Reference==
==Reference==
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Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme., Avalos JL, Bever KM, Wolberger C, Mol Cell. 2005 Mar 18;17(6):855-68. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15780941 15780941]
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Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme., Avalos JL, Bever KM, Wolberger C, Mol Cell. 2005 Mar 18;17(6):855-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15780941 15780941]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: sirtuin]]
[[Category: sirtuin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:20:59 2008''

Revision as of 13:21, 20 March 2008

Image:1yc5.gif


PDB ID 1yc5

Drag the structure with the mouse to rotate
, resolution 1.40Å
Ligands: and
Gene: npdA (Thermotoga maritima)
Coordinates: save as pdb, mmCIF, xml



Sir2-p53 peptide-nicotinamide


Contents

Overview

Sir2 enzymes form a unique class of NAD(+)-dependent deacetylases required for diverse biological processes, including transcriptional silencing, regulation of apoptosis, fat mobilization, and lifespan regulation. Sir2 activity is regulated by nicotinamide, a noncompetitive inhibitor that promotes a base-exchange reaction at the expense of deacetylation. To elucidate the mechanism of nicotinamide inhibition, we determined ternary complex structures of Sir2 enzymes containing nicotinamide. The structures show that free nicotinamide binds in a conserved pocket that participates in NAD(+) binding and catalysis. Based on our structures, we engineered a mutant that deacetylates peptides by using nicotinic acid adenine dinucleotide (NAAD) as a cosubstrate and is inhibited by nicotinic acid. The characteristics of the altered specificity enzyme establish that Sir2 enzymes contain a single site that participates in catalysis and nicotinamide regulation and provides additional insights into the Sir2 catalytic mechanism.

Disease

Known diseases associated with this structure: Adrenal cortical carcinoma OMIM:[191170], Breast cancer OMIM:[191170], Colorectal cancer OMIM:[191170], Hepatocellular carcinoma OMIM:[191170], Histiocytoma OMIM:[191170], Li-Fraumeni syndrome OMIM:[191170], Multiple malignancy syndrome OMIM:[191170], Nasopharyngeal carcinoma OMIM:[191170], Osteosarcoma OMIM:[191170], Pancreatic cancer OMIM:[191170], Thyroid carcinoma OMIM:[191170]

About this Structure

1YC5 is a Protein complex structure of sequences from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme., Avalos JL, Bever KM, Wolberger C, Mol Cell. 2005 Mar 18;17(6):855-68. PMID:15780941

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