1SLW
RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; NICKEL-BOUND
Summary for 1SLW
| Entry DOI | 10.2210/pdb1slw/pdb |
| Descriptor | ECOTIN, ANIONIC TRYPSIN, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | serine protease, inhibitor, complex, metal binding sites, protein engineering, protease-substrate interactions, metalloproteins, complex (serine protease-inhibitor) complex, complex (serine protease/inhibitor) |
| Biological source | Escherichia coli More |
| Cellular location | Periplasm: P23827 Secreted, extracellular space: P00763 |
| Total number of polymer chains | 2 |
| Total formula weight | 40207.33 |
| Authors | Brinen, L.S.,Fletterick, R.J. (deposition date: 1996-02-07, release date: 1996-07-11, Last modification date: 2024-10-30) |
| Primary citation | Brinen, L.S.,Willett, W.S.,Craik, C.S.,Fletterick, R.J. X-ray structures of a designed binding site in trypsin show metal-dependent geometry. Biochemistry, 35:5999-6009, 1996 Cited by PubMed Abstract: The three-dimensional structures of complexes of trypsin N143H, E151H bound to ecotin A86H are determined at 2.0 A resolution via X-ray crystallography in the absence and presence of the transition metals Zn2+, Ni2+, and Cu2+. The binding site for these transition metals was constructed by substitution of key amino acids with histidine at the trypsin-ecotin interface in the S2'/P2' pocket. Three histidine side chains, two on trypsin at positions 143 and 151 and one on ecotin at position 86, anchor the metals and provide extended catalytic recognition for substrates with His in the P2' pocket. Comparisons of the three-dimensional structures show the different geometries that result upon the binding of metal in the engineered tridentate site and suggest a structural basis for the kinetics of the metal-regulated catalysis. Of the three metals, the binding of zinc results in the most favorable binding geometry, not dissimilar to those observed in naturally occurring zinc binding proteins. PubMed: 8634241DOI: 10.1021/bi9530200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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