1n6q

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1n6q, resolution 3.Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HIV-1 Reverse Transcriptase Crosslinked to pre-translocation AZTMP-terminated DNA (complex N)

Overview

AZT (3'-azido-3'-deoxythymidine) resistance involves the enhanced excision, of AZTMP from the end of the primer strand by HIV-1 reverse transcriptase., This reaction can occur when an AZTMP-terminated primer is bound at the, nucleotide-binding site (pre-translocation complex N) but not at the, 'priming' site (post-translocation complex P). We determined the crystal, structures of N and P complexes at 3.0 and 3.1 A resolution. These, structures provide insight into the structural basis of AZTMP excision and, the mechanism of translocation. Docking of a dNTP in the P complex, structure suggests steric crowding in forming a stable ternary complex, that should increase the relative amount of the N complex, which is the, substrate for excision. Structural differences between complexes N and P, suggest that the conserved YMDD loop is involved in translocation, acting, as a springboard that helps to propel the primer terminus from the N to, the P site after dNMP incorporation.

About this Structure

1N6Q is a Protein complex structure of sequences from Human immunodeficiency virus 1 and Mus musculus with MG as ligand. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.

Reference

Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA., Sarafianos SG, Clark AD Jr, Das K, Tuske S, Birktoft JJ, Ilankumaran P, Ramesha AR, Sayer JM, Jerina DM, Boyer PL, Hughes SH, Arnold E, EMBO J. 2002 Dec 2;21(23):6614-24. PMID:12456667

Page seeded by OCA on Thu Nov 8 14:21:28 2007