3zxx

Structure of self-cleaved protease domain of PatA

spinqualitylabelsall models 3zxx, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zxx is a 1 chain structure with sequence from Prochloron didemni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q52QI9_PRODI Publication Abstract from PubMed Cyanobactins, including patellamides, are a group of cyanobacterial post-translationally modified ribosomal cyclic peptides. The final product should in theory be predictable from the sequence of the precursor peptide and the associated tailoring enzymes. Understanding the mechanism and recognition requirements of these enzymes will allow their rational engineering. We have identified three new cyanobactins from a Cyanothece PCC 7425 culture subjected to a heat shock. One of these compounds revealed a novel signature signal for ThcA, the subtilisin-like serine protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies allow rationalisation of the recognition determinants for both enzymes, consistent with the ribosomal biosynthetic origin of the new compounds. The Discovery of New Cyanobactins from Cyanothece PCC 7425 Defines a New Signature for Processing of Patellamides.,Houssen WE, Koehnke J, Zollman D, Vendome J, Raab A, Smith MC, Naismith JH, Jaspars M Chembiochem. 2012 Nov 21. doi: 10.1002/cbic.201200661. PMID:23169461 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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