2V9E
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248W-A273S)
Summary for 2V9E
| Entry DOI | 10.2210/pdb2v9e/pdb |
| Related | 1GT7 1OJR 2UYU 2UYV 2V29 2V2A 2V2B 2V9F 2V9G 2V9I 2V9L 2V9M |
| Descriptor | RHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | entropy index, metal-binding, oligomerization, zinc, lyase, aldolase, class ii, cytoplasm, cleavage of l-rhamnulose-1-phosphate to dihydroxyacetone, bacterial l-rhamnose metabolism, interface design, surface mutation, 2-ketose degradation, protein-protein interface, rare sugar, aggregation, zinc enzyme, fibrillation, rhamnose metabolism, protein engineering |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cytoplasm: P32169 |
| Total number of polymer chains | 2 |
| Total formula weight | 61066.47 |
| Authors | Grueninger, D.,Schulz, G.E. (deposition date: 2007-08-23, 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 (1.58 Å) |
Structure validation
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