1AVP

STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR

Summary for 1AVP

• Entry DOI: 10.2210/pdb1avp/pdb
• Descriptor: ADENOVIRAL PROTEINASE (3 entities in total)
• Functional Keywords: thiol hydrolase, viral proteinase, peptide cofactor, hydrolase
• Biological source: Human adenovirus 2; More
• Cellular location: Virion : P03252; Pre-protein VI: Host nucleus . Endosome lysis protein: Virion : P03274
• Total number of polymer chains: 2
• Total formula weight: 24467.99

Authors

Ding, J.,Mcgrath, W.J.,Sweet, R.M.,Mangel, W.F. (deposition date: 1996-04-04, release date: 1997-11-19, Last modification date: 2024-11-20)

Primary citation

Ding, J.,McGrath, W.J.,Sweet, R.M.,Mangel, W.F.
Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor.
EMBO J., 15:1778-1783, 1996

PubMed Abstract: The three-dimensional structure of the human adenovirus-2 proteinase complexed with its 11 amino acid cofactor, pVIc, was determined at 2.6 A resolution by X-ray crystallographic analysis. The fold of this protein has not been seen before. However, it represents an example of either subtly divergent or powerfully convergent evolution, because the active site contains a Cys-His-Glu triplet and oxyanion hole in an arrangement similar to that in papain. Thus, the adenovirus proteinase represents a new, fifth group of enzymes that contain catalytic triads. pVIc, which extends a beta-sheet in the main chain, is distant from the active site, yet its binding increases the catalytic rate constant 300-fold for substrate hydrolysis. The structure reveals several potential targets for antiviral therapy.

PubMed: 8617222

Experimental method

X-RAY DIFFRACTION (2.6 Å)