Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein.
Retroviral integrase, an essential enzyme for replication of human immunodeficiency virus type-1 (HIV-1) and other retroviruses, contains three structurally distinct domains, an N-terminal domain, the catalytic core and a C-terminal domain. To elucidate their spatial arrangement, we have solved the structure of a fragment of HIV-1 integrase comprising the N-terminal and catalytic core domains. This structure reveals a dimer interface between the N-terminal domains different from that observed for the isolated domain. It also complements the previously determined structure of the C-terminal two domains of HIV-1 integrase; superposition of the conserved catalytic core of the two structures results in a plausible full-length integrase dimer. Furthermore, an integrase tetramer formed by crystal lattice contacts bears structural resemblance to a related bacterial transposase, Tn5, and exhibits positively charged channels suitable for DNA binding.
Wang
J Y
JY
Laboratory of Molecular Biology, NIDDK, National Institutes of Health, 5 Center Drive MSC 0560, Bethesda, MD 20892, USA.
Ling
H
H
Yang
W
W
Craigie
R
R
D020134:Catalytic Domain; D019427:HIV Integrase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation
D010446:Peptide Fragments; D019427:HIV Integrase