3ZXX
Structure of self-cleaved protease domain of PatA
Summary for 3ZXX
| Entry DOI | 10.2210/pdb3zxx/pdb |
| Related | 3ZXY |
| Descriptor | SUBTILISIN-LIKE PROTEIN (2 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | PROCHLORON DIDEMNI |
| Total number of polymer chains | 1 |
| Total formula weight | 32369.54 |
| Authors | Koehnke, J.,Zollman, D.,Vendome, J.,Raab, A.,Houssen, W.E.,Smith, M.C.,Jaspars, M.,Naismith, J.H. (deposition date: 2011-08-16, release date: 2012-08-29, Last modification date: 2024-11-13) |
| Primary citation | Houssen, W.E.,Koehnke, J.,Zollman, D.,Vendome, J.,Raab, A.,Smith, M.C.,Naismith, J.H.,Jaspars, M. The Discovery of New Cyanobactins from Cyanothece Pcc 7425 Defines a New Signature for Processing of Patellamides. Chembiochem, 13:2683-, 2012 Cited by PubMed Abstract: 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. PubMed: 23169461DOI: 10.1002/CBIC.201200661 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
Download full validation report
