This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1s5p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1s5p.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1s5p.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1s5p| PDB=1s5p | SCENE= }}
{{STRUCTURE_1s5p| PDB=1s5p | SCENE= }}
-
'''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.===
-
==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.
+
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.
 +
-->
 +
{{ABSTRACT_PUBMED_15019790}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[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

Image:1s5p.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s5p"
Personal tools