4f5h | pdb_00004f5h

Intercoversion of Substrate Specificity: E. coli Aspatate Aminotransferase to Tyrosine Aminotransferase: Chimera P3.

spinqualitylabelsall models 4f5h, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f5h is a 2 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: LLP Related: 4f5f, 4f5g, 4f5i, 4f5j, 4f5k, 4f5l, 4f5m Gene: AAT, aspC, b0928, JW0911 (Escherichia coli K-12) Activity: Aspartate transaminase, with EC number 2.6.1.1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Identification of residues responsible for functional specificity in enzymes is a challenging and important problem in protein chemistry. Active-site residues are generally easy to identify, but residues outside the active site are also important to catalysis and their identities and roles are more difficult to determine. We report a method based on analysis of multiple sequence alignments, embodied in our program Janus, for predicting mutations required to interconvert structurally related but functionally distinct enzymes. Conversion of aspartate aminotransferase into tyrosine aminotransferase is demonstrated and compared to previous efforts. Incorporation of 35 predicted mutations resulted in an enzyme with the desired substrate specificity but low catalytic activity. A single round of DNA back-shuffling with wild-type aspartate aminotransferase on this variant generated mutants with tyrosine aminotransferase activities better than those previously realized from rational design or directed evolution. Methods such as this, coupled with computational modeling, may prove invaluable in furthering our understanding of enzyme catalysis and engineering. Janus: Prediction and Ranking of Mutations Required for Functional Interconversion of Enzymes.,Addington TA, Mertz RW, Siegel JB, Thompson JM, Fisher AJ, Filkov V, Fleischman N, Suen A, Zhang C, Toney MD J Mol Biol. 2013 Feb 6. pii: S0022-2836(13)00065-X. doi:, 10.1016/j.jmb.2013.01.034. PMID:23396064 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aspartate Aminotransferase

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