1T94

Crystal structure of the catalytic core of human DNA polymerase kappa

Summary for 1T94

• Entry DOI: 10.2210/pdb1t94/pdb
• Descriptor: polymerase (DNA directed) kappa (2 entities in total)
• Functional Keywords: replication; dna repair; y-family dna polymerase; translesion dna synthesis; lesion bypass, replication
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q9UBT6
• Total number of polymer chains: 2
• Total formula weight: 104805.58

Authors

Uljon, S.N.,Johnson, R.E.,Edwards, T.A.,Prakash, S.,Prakash, L.,Aggarwal, A.K. (deposition date: 2004-05-14, release date: 2004-08-31, Last modification date: 2024-02-14)

Primary citation

Uljon, S.N.,Johnson, R.E.,Edwards, T.A.,Prakash, S.,Prakash, L.,Aggarwal, A.K.
Crystal structure of the catalytic core of human DNA polymerase kappa.
STRUCTURE, 12:1395-1404, 2004

PubMed Abstract: We present the crystal structure of the catalytic core of human DNA polymerase kappa (hPolkappa), the first structure of a human Y-family polymerase. hPolkappa is implicated in the proficient extension of mispaired primer termini on undamaged DNAs, and in the extension step of lesion bypass. The structure reveals a stubby "fingers" subdomain, which despite its small size appears to be tightly restrained with respect to a putative templating base. The structure also reveals a novel "thumb" subdomain that provides a basis for the importance of the N-terminal extension unique to hPolkappa. And, most surprisingly, the structure reveals the polymerase-associated domain (PAD) juxtaposed on the dorsal side of the "palm" subdomain, as opposed to the fingers subdomain. Together, these properties suggest that the hPolkappa active site is constrained at the site of the templating base and incoming nucleotide, but the polymerase is less constrained following translocation of the lesion.

PubMed: 15296733
DOI: 10.1016/j.str.2004.05.011

Experimental method

X-RAY DIFFRACTION (2.4 Å)