From Proteopedia
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| - | [[Image:1s5p.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1s5p| PDB=1s5p | SCENE= }} | | {{STRUCTURE_1s5p| PDB=1s5p | SCENE= }} |
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| - | '''Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Eschericia coli.'''
| + | ===Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Eschericia coli.=== |
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| - | ==Overview==
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| - | Sirtuins are NAD+-dependent protein deacetylase enzymes that are broadly conserved from bacteria to human, and have been implicated to play important roles in gene regulation, metabolism and longevity. cobB is a bacterial sirtuin that deacetylates acetyl-CoA synthetase (Acs) at an active site lysine to stimulate its enzymatic activity. Here, we report the structure of cobB bound to an acetyl-lysine containing non-cognate histone H4 substrate. A comparison with the previously reported archaeal and eukaryotic sirtuin structures reveals the greatest variability in a small zinc-binding domain implicated to play a particularly important role in substrate-specific binding by the sirtuin proteins. Comparison of the cobB/histone H4 complex with other sirtuin proteins in complex with acetyl-lysine containing substrates, further suggests that contacts to the acetyl-lysine side-chain and beta-sheet interactions with residues directly C-terminal to the acetyl-lysine represent conserved features of sirtuin-substrate recognition. Isothermal titration calorimetry studies were used to compare the affinity of cobB for a variety of cognate and non-cognate acetyl-lysine-bearing peptides revealing an exothermic reaction with relatively little discrimination between substrates. In contrast, similar studies employing intact acetylated Acs protein as a substrate reveal a binding reaction that is endothermic, suggesting that cobB recognition of substrate involves a burial of hydrophobic surface and/or structural rearrangement involving substrate regions distal to the acetyl-lysine-binding site. Together, these studies suggest that substrate-specific binding by sirtuin proteins involves contributions from the zinc-binding domain of the enzyme and substrate regions distal to the acetyl-lysine-binding site.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15019790}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15019790 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15019790}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Protein deacetylase]] | | [[Category: Protein deacetylase]] |
| | [[Category: Sir2 homologue]] | | [[Category: Sir2 homologue]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:20:00 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:21:07 2008'' |
Revision as of 16:21, 28 July 2008
Template:STRUCTURE 1s5p
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Eschericia coli.
Template:ABSTRACT PUBMED 15019790
About this Structure
1S5P is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli., Zhao K, Chai X, Marmorstein R, J Mol Biol. 2004 Mar 26;337(3):731-41. PMID:15019790
Page seeded by OCA on Mon Jul 28 19:21:07 2008
