Summary for 6HWR
| Entry DOI | 10.2210/pdb6hwr/pdb |
| Descriptor | Fe(3+)-Zn(2+) purple acid phosphatase, TRIETHYLENE GLYCOL, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (19 entities in total) |
| Functional Keywords | purple acid phosphatase, metallohydrolases, transition state, catalysis, osteoporosis, metal binding protein |
| Biological source | Phaseolus vulgaris (Kidney bean) More |
| Total number of polymer chains | 4 |
| Total formula weight | 210461.13 |
| Authors | Feder, D.,Gahan, L.R.,McGeary, R.P.,Guddat, L.W.,Schenk, G. (deposition date: 2018-10-13, release date: 2019-04-03, Last modification date: 2024-10-23) |
| Primary citation | Feder, D.,Gahan, L.R.,McGeary, R.P.,Guddat, L.W.,Schenk, G. The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State. Chembiochem, 20:1536-1540, 2019 Cited by PubMed Abstract: Purple acid phosphatases (PAPs) are members of the large family of metallohydrolases, a group of enzymes that perform a wide range of biological functions, while employing a highly conserved catalytic mechanism. PAPs are found in plants, animals and fungi; in humans they play an important role in bone turnover and are thus of interest for developing treatments for osteoporosis. The majority of metallohydrolases use a metal-bound hydroxide to initiate catalysis, which leads to the formation of a proposed five-coordinate oxyphosphorane species in the transition state. In this work, we crystallized PAP from red kidney beans (rkbPAP) in the presence of both adenosine and vanadate. The in crystallo-formed vanadate analogue of ADP provides detailed insight into the binding mode of a PAP substrate, captured in a structure that mimics the putative fivecoordinate transition state. Our observations not only provide unprecedented insight into the mechanism of metallohydrolases, but might also guide the structure-based design of inhibitors for application in the treatment of several human illnesses. PubMed: 30719821DOI: 10.1002/cbic.201900077 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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