3A52
Crystal structure of cold-active alkailne phosphatase from psychrophile Shewanella sp.
Summary for 3A52
| Entry DOI | 10.2210/pdb3a52/pdb |
| Descriptor | Cold-active alkaline phosphatase, SULFATE ION, ZINC ION, ... (5 entities in total) |
| Functional Keywords | phosphatase, hydrolase |
| Biological source | Shewanella |
| Total number of polymer chains | 2 |
| Total formula weight | 86808.94 |
| Authors | Tsuruta, H.,Mikami, B.,Higashi, T.,Aizono, Y. (deposition date: 2009-07-24, release date: 2010-04-14, Last modification date: 2024-03-13) |
| Primary citation | Tsuruta, H.,Mikami, B.,Higashi, T.,Aizono, Y. Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp. Biosci.Biotechnol.Biochem., 74:69-74, 2010 Cited by PubMed Abstract: The crystal structure of a cold-active alkaline phosphatase from a psychrophile, Shewanella sp. (SCAP), was solved at 2.2 A. A refined model showed a homodimer with six metal-ligand sites. The arrangement of the catalytic residues resembled those of alkaline phosphatases (APs), suggesting that the reaction mechanism of SCAP was fundamentally identical to those of other APs. SCAP had two distinct structural features: (i) a loop with Arg122 that bound to the phosphate moiety of the substrate suffered no constraints from the linkage to other secondary structures, and (ii) Mg3-ligand His109 was considered to undergo repulsive effect with neighboring Trp228. The local flexibility led by these features might be an important factor in the high catalytic efficiency of SCAP at low temperatures. PubMed: 20057143DOI: 10.1271/bbb.90563 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
