1K6Y

Crystal Structure of a Two-Domain Fragment of HIV-1 Integrase

Summary for 1K6Y

• Entry DOI: 10.2210/pdb1k6y/pdb
• Descriptor: Integrase, ZINC ION, POTASSIUM ION, ... (5 entities in total)
• Functional Keywords: hiv-1, integrase, domain organization, transferase
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 4
• Total formula weight: 94075.87

Authors

Wang, J.,Ling, H.,Yang, W.,Craigie, R. (deposition date: 2001-10-17, release date: 2001-12-21, Last modification date: 2024-02-07)

Primary citation

Wang, J.Y.,Ling, H.,Yang, W.,Craigie, R.
Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein.
EMBO J., 20:7333-7343, 2001

PubMed Abstract: 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.

PubMed: 11743009
DOI: 10.1093/emboj/20.24.7333

Experimental method

X-RAY DIFFRACTION (2.4 Å)