2w5e | pdb_00002w5e

Structural and biochemical analysis of human pathogenic astrovirus serine protease at 2.0 Angstrom resolution

spinqualitylabelsall models 2w5e, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2w5e is a 6 chain structure with sequence from Human astrovirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: CD, CL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3ZN04_HASV1 Protein covalently attached to the 5' extremity of the genomic and subgenomic RNAs.[ARBA:ARBA00029406] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Astroviruses are single-stranded RNA viruses with a replication strategy based on the proteolytic processing of a polyprotein precursor and subsequent release of the viral enzymes of replication. So far, the catalytic properties of the astrovirus protease as well as its structure have remained uncharacterized. In this study, the three-dimensional crystal structure of the predicted protease of human pathogenic astrovirus has been solved to 2.0 A resolution. The protein displays the typical properties of trypsin-like enzymes but also several characteristic features: (i) a catalytic Asp-His-Ser triad in which the aspartate side chain is oriented away from the histidine, being replaced by a water molecule; (ii) a non-common conformation and composition of the S1 pocket; and (iii) the lack of the typical surface beta-ribbons together with a "featureless" shape of the substrate-binding site. Hydrolytic activity assays indicate that the S1 pocket recognises Glu and Asp side chains specifically, which, therefore, are predicted to occupy the P1 position on the substrate cleavage site. The positive electrostatic potential featured by the S1 region underlies this specificity. The comparative structural analysis highlights the peculiarity of the astrovirus protease, and differentiates it from the human and viral serine proteases. Structural and biochemical analysis of human pathogenic astrovirus serine protease at 2.0 A resolution.,Speroni S, Rohayem J, Nenci S, Bonivento D, Robel I, Barthel J, Luzhkov VB, Coutard B, Canard B, Mattevi A J Mol Biol. 2009 Apr 17;387(5):1137-52. Epub 2009 Feb 26. PMID:19249313 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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