Summary information and primary citation
- PDB-id
-
3tq1;
DSSR-derived features in text and
JSON formats
- Class
- transferase-DNA
- Method
- X-ray (2.556 Å)
- Summary
- Human DNA polymerase eta in binary complex with
DNA
- Reference
-
Ummat A, Silverstein TD, Jain R, Buku A, Johnson RE,
Prakash L, Prakash S, Aggarwal AK (2012): "Human DNA
Polymerase Eta Is Pre-Aligned for dNTP Binding and
Catalysis." J.Mol.Biol.,
415, 627-634. doi: 10.1016/j.jmb.2011.11.038.
- Abstract
- Pre-steady-state kinetic studies on Y-family DNA
polymerase η (Polη) have suggested that the polymerase
undergoes a rate-limiting conformational change step before
the phosphoryl transfer of the incoming nucleotide to the
primer terminus. However, the nature of this rate-limiting
conformational change step has been unclear, due in part to
the lack of structural information on the Polη binary
complex. We present here for the first time a crystal
structure of human Polη (hPolη) in binary complex with its
DNA substrate. We show that the hPolη domains move only
slightly on dNTP binding and that the polymerase by and
large is pre-aligned for dNTP binding and catalysis. We
also show that there is no major reorientation of the DNA
from a nonproductive to a productive configuration and that
the active site is devoid of metals in the absence of dNTP.
Together, these observations lead us to suggest that the
rate-limiting conformational change step in the Polη
replication cycle likely corresponds to a rate-limiting
entry of catalytic metals in the active site.
