4D74
1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI
Summary for 4D74
| Entry DOI | 10.2210/pdb4d74/pdb |
| Descriptor | PROTEIN-TYROSINE-PHOSPHATASE AMSI, SULFATE ION (3 entities in total) |
| Functional Keywords | hydrolase, amylovoran, tyrosine phosphatase, phosphatase, amsi, fire blight |
| Biological source | ERWINIA AMYLOVORA |
| Total number of polymer chains | 1 |
| Total formula weight | 19200.89 |
| Authors | Benini, S.,Salomone-Stagni, M.,Caputi, L.,Cianci, M. (deposition date: 2014-11-19, release date: 2016-01-20, Last modification date: 2023-12-20) |
| Primary citation | Salomone-Stagni, M.,Musiani, F.,Benini, S. Characterization and 1.57 A Resolution Structure of the Key Fire Blight Phosphatase Amsi from Erwinia Amylovora Acta Crystallogr.,Sect.F, 72:903-, 2016 Cited by PubMed Abstract: AmsI is a low-molecular-weight protein tyrosine phosphatase that regulates the production of amylovoran in the Gram-negative bacterium Erwinia amylovora, a specific pathogen of rosaceous plants such as apple, pear and quince. Amylovoran is an exopolysaccharide that is necessary for successful infection. In order to shed light on AmsI, its structure was solved at 1.57 Å resolution at the same pH as its highest measured activity (pH 5.5). In the active site, a water molecule, bridging between the catalytic Arg15 and the reaction-product analogue sulfate, might be representative of the water molecule attacking the phospho-cysteine intermediate in the second step of the reaction mechanism. PubMed: 27917839DOI: 10.1107/S2053230X16018781 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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