Backbone assignment of the little finger domain of a Y-family DNA polymerase.

Abstract:

:Sulfolobus solfataricus DNA polymerase IV (Dpo4), a prototype Y-family DNA polymerase, contains a unique little finger domain besides a catalytic core. Here, we report the chemical shift assignments for the backbone nitrogens, α and β carbons, and amide protons of the little finger domain of Dpo4. This work and our published backbone assignment for the catalytic core provide the basis for investigating the conformational dynamics of Dpo4 during catalysis using solution NMR spectroscopy.

journal_name

Biomol NMR Assign

authors

Ma D,Fowler JD,Suo Z

doi

10.1007/s12104-011-9298-1

subject

Has Abstract

pub_date

2011-10-01 00:00:00

pages

195-8

issue

2

eissn

1874-2718

issn

1874-270X

journal_volume

5

pub_type

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