4qys | pdb_00004qys

TrpB2 enzymes

spinqualitylabelsall models 4qys, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qys is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLP, PLR, SEP Activity: Tryptophan synthase, with EC number 4.2.1.20 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TRPB2_SULSO] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. Publication Abstract from PubMed The rapid increase of the number of sequenced genomes asks for the functional annotation of the encoded enzymes. We used a combined computational-structural approach to determine the function of the TrpB2 subgroup of the tryptophan synthase beta chain/beta chain-like TrpB1-TrpB2 family (IPR023026). The results showed that TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases, whereas TrpB1 enzymes catalyze the l-serine dependent synthesis of tryptophan. We found a single residue being responsible for the different substrate specificities of TrpB1 and TrpB2 and confirmed this finding by mutagenesis studies and crystallographic analysis of a TrpB2 enzyme with bound O-phospho-l-serine. TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases.,Busch F, Rajendran C, Mayans O, Loffler P, Merkl R, Sterner R Biochemistry. 2014 Sep 30;53(38):6078-83. doi: 10.1021/bi500977y. Epub 2014 Sep, 17. PMID:25184516 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tryptophan synthase

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