1taq
From Proteopedia
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| - | [[Image:1taq.gif|left|200px]] | + | [[Image:1taq.gif|left|200px]] |
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| - | '''STRUCTURE OF TAQ DNA POLYMERASE''' | + | {{Structure |
| + | |PDB= 1taq |SIZE=350|CAPTION= <scene name='initialview01'>1taq</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] | ||
| + | |GENE= TAQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 Thermus aquaticus]) | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF TAQ DNA POLYMERASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TAQ is a [ | + | 1TAQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAQ OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of Thermus aquaticus DNA polymerase., Kim Y, Eom SH, Wang J, Lee DS, Suh SW, Steitz TA, Nature. 1995 Aug 17;376(6541):612-6. PMID:[http:// | + | Crystal structure of Thermus aquaticus DNA polymerase., Kim Y, Eom SH, Wang J, Lee DS, Suh SW, Steitz TA, Nature. 1995 Aug 17;376(6541):612-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7637814 7637814] |
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: taq dna polymerase]] | [[Category: taq dna polymerase]] | ||
| - | ''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 14:16:04 2008'' |
Revision as of 12:16, 20 March 2008
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | TAQ (Thermus aquaticus) | ||||||
| Activity: | DNA-directed DNA polymerase, with EC number 2.7.7.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF TAQ DNA POLYMERASE
Overview
The DNA polymerase from Thermus aquaticus (Taq polymerase), famous for its use in the polymerase chain reaction, is homologous to Escherichia coli DNA polymerase I (pol I) Like pol I, Taq polymerase has a domain at its amino terminus (residues 1-290) that has 5' nuclease activity and a domain at its carboxy terminus that catalyses the polymerase reaction. Unlike pol I, the intervening domain in Taq polymerase has lost the editing 3'-5' exonuclease activity. Although the structure of the Klenow fragment of pol I has been known for ten years, that of the intact pol I has proved more elusive. The structure of Taq polymerase determined here at 2.4 A resolution shows that the structures of the polymerase domains of the thermostable enzyme and of the Klenow fragment are nearly identical, whereas the catalytically critical carboxylate residues that bind two metal ions are missing from the remnants of the 3'-5' exonuclease active site of Taq polymerase. The first view of the 5' nuclease domain, responsible for excising the Okazaki RNA in lagging-strand DNA replication, shows a cluster of conserved divalent metal-ion-binding carboxylates at the bottom of a cleft. The location of this 5'-nuclease active site some 70 A from the polymerase active site in this crystal form highlights the unanswered question of how this domain works in concert with the polymerase domain to produce a duplex DNA product that contains only a nick.
About this Structure
1TAQ is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.
Reference
Crystal structure of Thermus aquaticus DNA polymerase., Kim Y, Eom SH, Wang J, Lee DS, Suh SW, Steitz TA, Nature. 1995 Aug 17;376(6541):612-6. PMID:7637814
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