1xo1
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Exodeoxyribonuclease_(lambda-induced) Exodeoxyribonuclease (lambda-induced)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.3 3.1.11.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_(lambda-induced) Exodeoxyribonuclease (lambda-induced)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.3 3.1.11.3] </span> |
| - | |GENE= D15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= D15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10726 Enterobacteria phage T5]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xo1 OCA], [http://www.ebi.ac.uk/pdbsum/1xo1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xo1 RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XO1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1XO1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t5 Enterobacteria phage t5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XO1 OCA]. |
==Reference== | ==Reference== | ||
Mutagenesis of conserved lysine residues in bacteriophage T5 5'-3' exonuclease suggests separate mechanisms of endo-and exonucleolytic cleavage., Garforth SJ, Ceska TA, Suck D, Sayers JR, Proc Natl Acad Sci U S A. 1999 Jan 5;96(1):38-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9874768 9874768] | Mutagenesis of conserved lysine residues in bacteriophage T5 5'-3' exonuclease suggests separate mechanisms of endo-and exonucleolytic cleavage., Garforth SJ, Ceska TA, Suck D, Sayers JR, Proc Natl Acad Sci U S A. 1999 Jan 5;96(1):38-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9874768 9874768] | ||
| + | [[Category: Enterobacteria phage t5]] | ||
[[Category: Exodeoxyribonuclease (lambda-induced)]] | [[Category: Exodeoxyribonuclease (lambda-induced)]] | ||
| - | [[Category: Pseudomonas phage d3112]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ceska, T A.]] | [[Category: Ceska, T A.]] | ||
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[[Category: nuclease]] | [[Category: nuclease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:52:18 2008'' |
Revision as of 21:52, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | D15 (Enterobacteria phage T5) | ||||||
| Activity: | Exodeoxyribonuclease (lambda-induced), with EC number 3.1.11.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
T5 5'-EXONUCLEASE MUTANT K83A
Overview
Efficient cellular DNA replication requires the activity of a 5'-3' exonuclease. These enzymes are able to hydrolyze DNA.DNA and RNA.DNA substrates exonucleolytically, and they are structure-specific endonucleases. The 5'-3' exonucleases are conserved in organisms as diverse as bacteriophage and mammals. Crystal structures of three representative enzymes identify two divalent-metal-binding sites typically separated by 8-10 A. Site-directed mutagenesis was used to investigate the roles of three lysine residues (K83, K196, and K215) situated near two metal-binding sites in bacteriophage T5 5'-3' exonuclease. Neither K196 nor K215 was essential for either the exo- or the endonuclease activity, but mutation of these residues increased the dissociation constant for the substrate from 5 nM to 200 nM (K196A) and 50 nM (K215A). Biochemical analysis demonstrated that K83 is absolutely required for exonucleolytic activity on single-stranded DNA but is not required for endonucleolytic cleavage of flap structures. Structural analysis of this mutant by x-ray crystallography showed no significant perturbations around the metal-binding sites in the active site. The wild-type protein has different pH optima for endonuclease and exonuclease activities. Taken together, these results suggest that different mechanisms for endo- and exonucleolytic hydrolysis are used by this multifunctional enzyme.
About this Structure
1XO1 is a Single protein structure of sequence from Enterobacteria phage t5. Full crystallographic information is available from OCA.
Reference
Mutagenesis of conserved lysine residues in bacteriophage T5 5'-3' exonuclease suggests separate mechanisms of endo-and exonucleolytic cleavage., Garforth SJ, Ceska TA, Suck D, Sayers JR, Proc Natl Acad Sci U S A. 1999 Jan 5;96(1):38-43. PMID:9874768
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