1tgo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS== | ==THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS== | ||
<StructureSection load='1tgo' size='340' side='right' caption='[[1tgo]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1tgo' size='340' side='right'caption='[[1tgo]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1tgo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700654 Atcc 700654]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TGO FirstGlance]. <br> | <table><tr><td colspan='2'>[[1tgo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700654 Atcc 700654]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TGO FirstGlance]. <br> | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[DNA polymerase|DNA polymerase]] | *[[DNA Polymerase in Thermococcus gorgonarius|DNA Polymerase in Thermococcus gorgonarius]] | ||
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 37: | Line 38: | ||
[[Category: Atcc 700654]] | [[Category: Atcc 700654]] | ||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Large Structures]] | |||
[[Category: Angerer, B]] | [[Category: Angerer, B]] | ||
[[Category: Ankenbauer, W]] | [[Category: Ankenbauer, W]] | ||
Revision as of 16:45, 18 December 2019
THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUSTHERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS
Structural highlights
Function[DPOL_THEGO] In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMost 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||