1b04
From Proteopedia
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- | [[Image:1b04.gif|left|200px]] | + | [[Image:1b04.gif|left|200px]] |
- | + | ||
- | '''STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE''' | + | {{Structure |
+ | |PDB= 1b04 |SIZE=350|CAPTION= <scene name='initialview01'>1b04</scene>, resolution 2.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/DNA_ligase_(NAD(+)) DNA ligase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.2 6.5.1.2] | ||
+ | |GENE= LIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus]) | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1B04 is a [ | + | 1B04 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B04 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10368271 10368271] |
[[Category: DNA ligase (NAD(+))]] | [[Category: DNA ligase (NAD(+))]] | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
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[[Category: ligase]] | [[Category: ligase]] | ||
- | ''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 10:04:31 2008'' |
Revision as of 08:04, 20 March 2008
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, resolution 2.8Å | |||||||
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Gene: | LIG (Geobacillus stearothermophilus) | ||||||
Activity: | DNA ligase (NAD(+)), with EC number 6.5.1.2 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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.
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
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