1yg9: Difference between revisions
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==The structure of mutant (N93Q) of bla g 2== | ==The structure of mutant (N93Q) of bla g 2== | ||
<StructureSection load='1yg9' size='340' side='right' caption='[[1yg9]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='1yg9' size='340' side='right'caption='[[1yg9]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1yg9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Blage Blage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YG9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YG9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1yg9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Blage Blage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YG9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YG9 FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Blage]] | [[Category: Blage]] | ||
[[Category: Large Structures]] | |||
[[Category: Gustchina, A]] | [[Category: Gustchina, A]] | ||
[[Category: Li, M]] | [[Category: Li, M]] |
Revision as of 19:33, 29 January 2020
The structure of mutant (N93Q) of bla g 2The structure of mutant (N93Q) of bla g 2
Structural highlights
Function[ASP2_BLAGE] Functions as a digestive enzyme in the cockroach. 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 PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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