8y98

Crystal structure of a heterooligomeric aminotransferase from Serratia sp. ATCC 39006, PPE-bound form

spinqualitylabelsall models 8y98, resolution 2.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8y98 is a 4 chain structure with sequence from Serratia sp. ATCC 39006. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.31Å Ligands: PGU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2I5T5Y7_SERS3 Publication Abstract from PubMed Serratia sp. ATCC 39006 has two tandemly positioned genes, ser4 and ser5, both annotated as sugar aminotransferases, in a putative secondary metabolite biosynthetic gene cluster. Ser5 possesses a complete fold-type I aminotransferase fold, while Ser4 lacks the N- and C-terminal regions and a catalytically important lysine residue of fold-type I aminotransferase. We herein revealed that Ser4 and Ser5 formed a heterotetrameric complex (SerTA) with aminotransferase activity and determined the crystal structures. MD simulations and activity assays with SerTA variants indicated that residues from helix alpha-8* of inactive Ser4 are important for activity, confirming the importance of heterocomplex formation for activity. Furthermore, the structures suggest that SerTA recognizes a substrate loaded on the carrier protein. Crystal structure of a novel heterooligomeric aminotransferase from Serratia sp. ATCC 39006 provides insights into function.,Pramono H, Yoshida A, Hirashima Y, Sone Y, Terada T, Kosono S, Nishiyama M FEBS Lett. 2024 Dec 1. doi: 10.1002/1873-3468.15068. PMID:39618122 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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