1s5p
From Proteopedia
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| - | [[Image:1s5p.gif|left|200px]] | + | [[Image:1s5p.gif|left|200px]] |
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| - | '''Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Eschericia coli.''' | + | {{Structure |
| + | |PDB= 1s5p |SIZE=350|CAPTION= <scene name='initialview01'>1s5p</scene>, resolution 1.96Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= NPDA, COBB, B1120 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Eschericia coli.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S5P is a [ | + | 1S5P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5P OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15019790 15019790] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sir2 homologue]] | [[Category: sir2 homologue]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:48 2008'' |
Revision as of 12:00, 20 March 2008
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| , resolution 1.96Å | |||||||
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| Ligands: | |||||||
| Gene: | NPDA, COBB, B1120 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Eschericia coli.
Overview
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.
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
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