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.


1b04

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1b04.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1b04.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1b04| PDB=1b04 | SCENE= }}
{{STRUCTURE_1b04| PDB=1b04 | SCENE= }}
-
'''STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE'''
+
===STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE===
-
==Overview==
+
<!--
-
BACKGROUND: DNA ligases catalyse phosphodiester bond formation between adjacent bases in nicked DNA, thereby sealing the nick. A key step in the catalytic mechanism is the formation of an adenylated DNA intermediate. The adenyl group is derived from either ATP (in eucaryotes and archaea) or NAD+4 (in bacteria). This difference in cofactor specificity suggests that DNA ligase may be a useful antibiotic target. RESULTS: The crystal structure of the adenylation domain of the NAD+-dependent DNA ligase from Bacillus stearothermophilus has been determined at 2.8 A resolution. Despite a complete lack of detectable sequence similarity, the fold of the central core of this domain shares homology with the equivalent region of ATP-dependent DNA ligases, providing strong evidence for the location of the NAD+-binding site. CONCLUSIONS: Comparison of the structure of the NAD+4-dependent DNA ligase with that of ATP-dependent ligases and mRNA-capping enzymes demonstrates the manifold utilisation of a conserved nucleotidyltransferase domain within this family of enzymes. Whilst this conserved core domain retains a common mode of nucleotide binding and activation, it is the additional domains at the N terminus and/or the C terminus that provide the alternative specificities and functionalities in the different members of this enzyme superfamily.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10368271}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10368271 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10368271}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Dna replication]]
[[Category: Dna replication]]
[[Category: Ligase]]
[[Category: Ligase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:54:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:57:19 2008''

Revision as of 14:57, 30 June 2008

Image:1b04.png

Template:STRUCTURE 1b04

STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE

Template:ABSTRACT PUBMED 10368271

About this Structure

1B04 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

Structure of the adenylation domain of an NAD+-dependent DNA ligase., Singleton MR, Hakansson K, Timson DJ, Wigley DB, Structure. 1999 Jan 15;7(1):35-42. PMID:10368271

Page seeded by OCA on Mon Jun 30 17:57:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b04"
Personal tools