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PolD DNA Polymerase, Pyrococcus horikoshii

 
National Institutes of Health

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Broader (2)

Archaeal ProteinsDNA-Directed DNA Polymerase

Papers overview

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2019
2019
Structure of the DP1–DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases
PolD is an archaeal replicative DNA polymerase (DNAP) made of a proofreading exonuclease subunit (DP1) and a larger polymerase… Expand
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2015
2015
Pre-steady-state Kinetic Analysis of a Family D DNA Polymerase from Thermococcus sp. 9°N Reveals Mechanisms for Archaeal Genomic Replication and Maintenance*
Background: Family D DNA polymerase (polD) is important for replication in most archaea, excluding Crenarchaeota. Results: We… Expand
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2012
2012
NMR and crystal structures of the Pyrococcus horikoshii RadA intein guide a strategy for engineering a highly efficient and promiscuous intein.
In protein splicing, an intervening protein sequence (intein) in the host protein excises itself out and ligates two split host… Expand
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2010
2010
Reconstitution of diphthine synthase activity in vitro.
Diphthamide, the target of diphtheria toxin, is a unique posttranslational modification on eukaryotic and archaeal translation… Expand
2009
2009
Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii
Prolidases hydrolyze the unique bond between X-Pro dipeptides and can also cleave the P–F and P–O bonds found in organophosphorus… Expand
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2009
2009
Erratum to: Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii
Fig. 2 Activity of P. horikoshii prolidases over a pH range of 4.0–10.0. Prolidase assays contained 14.8 ng for Phprol and 6.2 ng… Expand
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2008
2008
Crystallographic and mutational studies of seryl-tRNA synthetase from the archaeon Pyrococcus horikoshii
Seryl-tRNA synthetase (SerRS) catalyzes the ligation of serine to the 3′-end of serine tRNA (tRNASer), which is typical of the… Expand
2007
2007
Structure of an archaeal TYW1, the enzyme catalyzing the second step of wye-base biosynthesis.
Wye bases are tricyclic bases that are found in archaeal and eukaryotic tRNAs. The most modified wye base, wybutosine, which… Expand
2005
2005
Cloning and Characterization of the Thymidylate Synthase Complementing Protein from Environmental Parachlamydia
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