1FMB

EIAV PROTEASE COMPLEXED WITH THE INHIBITOR HBY-793

Summary for 1FMB

• Entry DOI: 10.2210/pdb1fmb/pdb
• Descriptor: EIAV PROTEASE, [2-(2-METHYL-PROPANE-2-SULFONYLMETHYL)-3-NAPHTHALEN-1-YL-PROPIONYL-VALINYL]-PHENYLALANINOL (3 entities in total)
• Functional Keywords: hydrolase (acid proteinase), rna-directed dna polymerase, aspartyl protease, endonuclease, polyprotein
• Biological source: Equine infectious anemia virus
• Total number of polymer chains: 1
• Total formula weight: 11959.02

Authors

Wlodawer, A.,Gustchina, A.,Zdanov, A.,Kervinen, J. (deposition date: 1996-02-27, release date: 1996-10-14, Last modification date: 2024-04-03)

Primary citation

Gustchina, A.,Kervinen, J.,Powell, D.J.,Zdanov, A.,Kay, J.,Wlodawer, A.
Structure of equine infectious anemia virus proteinase complexed with an inhibitor.
Protein Sci., 5:1453-1465, 1996

PubMed Abstract: Equine infectious anemia virus (EIAV), the causative agent of infectious anemia in horses, is a member of the lentiviral family. The virus-encoded proteinase (PR) processes viral polyproteins into functional molecules during replication and it also cleaves viral nucleocapsid protein during infection. The X-ray structure of a complex of the 154G mutant of EIAV PR with the inhibitor HBY-793 was solved at 1.8 A resolution and refined to a crystallographic R-factor of 0.136. The molecule is a dimer in which the monomers are related by a crystallographic twofold axis. Although both the enzyme and the inhibitor are symmetric, the interactions between the central part of the inhibitor and the active site aspartates are asymmetric, and the inhibitor and the two flaps are partially disordered. The overall fold of EIAV PR is very similar to that of other retroviral proteinases. However, a novel feature of the EIAV PR structure is the appearance of the second alpha-helix in the monomer in a position predicted by the structural template for the family of aspartic proteinases. The parts of the EIAV PR with the highest resemblance to human immunodeficiency virus type 1 PR include the substrate-binding sites; thus, the differences in the specificity of both enzymes have to be explained by enzyme-ligand interactions at the periphery of the active site as well.

PubMed: 8844837

Experimental method

X-RAY DIFFRACTION (1.8 Å)