We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
2kxe
From Proteopedia
Revision as of 04:22, 29 September 2014 by OCA (Talk | contribs)
2kxe is a 1 chain structure with sequence from Pyrococcus horikoshii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Archaea-specific D-family DNA polymerase forms a heterotetramer consisting of two large polymerase subunits and two small exonuclease subunits. We analyzed the structure of the N-terminal 200 amino-acid regulatory region of the small subunit by NMR and revealed that the N-terminal approximately 70 amino-acid region is folded. The structure consists of a four-alpha-helix bundle including a short parallel beta-sheet, which is similar to the N-terminal regions of the B subunits of human DNA polymerases alpha and epsilon, establishing evolutionary relationships among these archaeal and eukaryotic polymerases. We observed monomer-dimer equilibrium of this domain, which may be related to holoenzyme architecture and/or functional regulation.
Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases.,Yamasaki K, Urushibata Y, Yamasaki T, Arisaka F, Matsui I FEBS Lett. 2010 Aug 4;584(15):3370-5. Epub 2010 Jun 23. PMID:20598295[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Yamasaki K, Urushibata Y, Yamasaki T, Arisaka F, Matsui I. Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases. FEBS Lett. 2010 Aug 4;584(15):3370-5. Epub 2010 Jun 23. PMID:20598295 doi:10.1016/j.febslet.2010.06.026
