2jug | pdb_00002jug

Multienzyme Docking in Hybrid Megasynthetases

spinqualitylabelsall models 2jug, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jug is a 2 chain structure with sequence from Angiococcus disciformis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: tubC (Angiococcus disciformis) 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 Hybrid multienzyme systems composed of polyketide synthase (PKS) and nonribosomal polypeptide synthetase (NRPS) modules direct the biosynthesis of clinically valuable natural products in bacteria. The fidelity of this process depends on specific recognition between successive polypeptides in each assembly line-interactions that are mediated by terminal 'docking domains'. We have identified a new family of N-terminal docking domains, exemplified by TubCdd from the tubulysin system of Angiococcus disciformis An d48. TubCdd is homodimeric, which suggests that NRPS subunits in mixed systems self-associate to interact with partner PKS homodimers. The NMR structure of TubCdd reveals a new fold featuring an exposed beta-hairpin that serves as the binding site for the C-terminal docking domain of the partner polypeptide. The pattern of charged residues on the contact surface of the beta-hairpin is a key determinant of the interaction and seems to constitute a 'docking code' that can be used to alter binding affinity. Multienzyme docking in hybrid megasynthetases.,Richter CD, Nietlispach D, Broadhurst RW, Weissman KJ Nat Chem Biol. 2008 Jan;4(1):75-81. Epub 2007 Dec 9. PMID:18066054 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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