1yg9

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Revision as of 04:37, 21 November 2007

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spinqualitylabelsall models 1yg9, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The structure of mutant (N93Q) of bla g 2

Overview

The crystal structure of Bla g 2 was solved in order to investigate the, structural basis for the allergenic properties of this unusual protein., This is the first structure of an aspartic protease in which conserved, glycine residues, in two canonical DTG triads, are substituted by, different amino acid residues. Another unprecedented feature revealed by, the structure is the single phenylalanine residue insertion on the tip of, the flap, with the side-chain occupying the S1 binding pocket. This and, other important amino acid substitutions in the active site region of Bla, g 2 modify the interactions in the vicinity of the catalytic aspartate, residues, increasing the distance between them to approximately 4A and, establishing unique direct contacts between the flap and the catalytic, residues. We attribute the absence of substantial catalytic activity in, Bla g 2 to these unusual features of the active site. Five disulfide, bridges and a Zn-binding site confer stability to the protein, which may, contribute to sensitization at lower levels of exposure than other, allergens.

About this Structure

1YG9 is a Single protein structure of sequence from Blattella germanica with NAG and ZN as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of cockroach allergen Bla g 2, an unusual zinc binding aspartic protease with a novel mode of self-inhibition., Gustchina A, Li M, Wunschmann S, Chapman MD, Pomes A, Wlodawer A, J Mol Biol. 2005 Apr 29;348(2):433-44. PMID:15811379

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