1avp
From Proteopedia
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| , resolution 2.6Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR
Overview
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.
About this Structure
1AVP is a Protein complex structure of sequences from Human adenovirus 2. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor., Ding J, McGrath WJ, Sweet RM, Mangel WF, EMBO J. 1996 Apr 15;15(8):1778-83. PMID:8617222
Page seeded by OCA on Sun Mar 30 18:48:23 2008
