2V7G
Crystal Structure of an Engineered Urocanase Tetramer
Summary for 2V7G
| Entry DOI | 10.2210/pdb2v7g/pdb |
| Related | 1UWK 1UWL 1W1U |
| Descriptor | UROCANATE HYDRATASE, ACETATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | histidine degradation, nad, lyase, protein engineering, urocanate hydratase, histidine metabolism |
| Biological source | PSEUDOMONAS PUTIDA |
| Cellular location | Cytoplasm: P25080 |
| Total number of polymer chains | 4 |
| Total formula weight | 247142.59 |
| Authors | Treiber, N.,Schulz, G.E. (deposition date: 2007-07-30, release date: 2008-01-15, Last modification date: 2023-12-13) |
| Primary citation | Grueninger, D.,Treiber, N.,Ziegler, M.O.P.,Koetter, J.W.A.,Schulze, M.-S.,Schulz, G.E. Designed Protein-Protein Association. Science, 319:206-, 2008 Cited by PubMed Abstract: The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side-chain alteration in order to associate to a higher-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures. PubMed: 18187656DOI: 10.1126/SCIENCE.1150421 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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