9gaa | pdb_00009gaa

PRECURSOR OF THE T152A MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM

spinqualitylabelsall models 9gaa, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9gaa is a 2 chain structure with sequence from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 Resources: FirstGlance, OCA, RCSB, PDBsum 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 A variety of proteins, including glycosylasparaginase, have recently been found to activate functions by self-catalyzed peptide bond rearrangements from single-chain precursors. Here we present the 1.9 A crystal structures of glycosylasparaginase precursors that are able to autoproteolyze via an N --> O acyl shift. Several conserved residues are aligned around the scissile peptide bond that is in a highly strained trans peptide bond configuration. The structure illustrates how a nucleophilic side chain may attack the scissile peptide bond at the immediate upstream backbone carbonyl and provides an understanding of the structural basis for peptide bond cleavage via an N --> O or N --> S acyl shift that is used by various groups of intramolecular autoprocessing proteins. Structural insights into the mechanism of intramolecular proteolysis.,Xu Q, Buckley D, Guan C, Guo HC Cell. 1999 Sep 3;98(5):651-61. PMID:10490104 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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