1tgo

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[[Image:1tgo.jpg|left|200px]]
[[Image:1tgo.jpg|left|200px]]
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{{Structure
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|PDB= 1tgo |SIZE=350|CAPTION= <scene name='initialview01'>1tgo</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1tgo", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1tgo| PDB=1tgo | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tgo OCA], [http://www.ebi.ac.uk/pdbsum/1tgo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tgo RCSB]</span>
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'''THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS'''
'''THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS'''
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[[Category: Huber, R.]]
[[Category: Huber, R.]]
[[Category: Laue, F.]]
[[Category: Laue, F.]]
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[[Category: disulfide bond]]
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[[Category: Disulfide bond]]
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[[Category: dna polymerase]]
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[[Category: Dna polymerase]]
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[[Category: replication]]
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[[Category: Replication]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:55:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:48 2008''
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Revision as of 06:55, 3 May 2008

Image:1tgo.jpg

Template:STRUCTURE 1tgo

THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS


Overview

Most known archaeal DNA polymerases belong to the type B family, which also includes the DNA replication polymerases of eukaryotes, but maintain high fidelity at extreme conditions. We describe here the 2.5 A resolution crystal structure of a DNA polymerase from the Archaea Thermococcus gorgonarius and identify structural features of the fold and the active site that are likely responsible for its thermostable function. Comparison with the mesophilic B type DNA polymerase gp43 of the bacteriophage RB69 highlights thermophilic adaptations, which include the presence of two disulfide bonds and an enhanced electrostatic complementarity at the DNA-protein interface. In contrast to gp43, several loops in the exonuclease and thumb domains are more closely packed; this apparently blocks primer binding to the exonuclease active site. A physiological role of this "closed" conformation is unknown but may represent a polymerase mode, in contrast to an editing mode with an open exonuclease site. This archaeal B DNA polymerase structure provides a starting point for structure-based design of polymerases or ligands with applications in biotechnology and the development of antiviral or anticancer agents.

About this Structure

1TGO is a Single protein structure of sequence from Thermococcus gorgonarius. Full crystallographic information is available from OCA.

Reference

Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius., Hopfner KP, Eichinger A, Engh RA, Laue F, Ankenbauer W, Huber R, Angerer B, Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3600-5. PMID:10097083 Page seeded by OCA on Sat May 3 09:55:47 2008

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