Structural highlights
6hwr is a 4 chain structure with sequence from Phaseolus vulgaris. This structure supersedes the now removed PDB entry 4kkz. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Method: | X-ray diffraction, Resolution 1.95Å |
Ligands: | , , , , , , , , , , , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PPAF_PHAVU
Publication Abstract from PubMed
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.
The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State.,Feder D, Gahan LR, McGeary RP, Guddat LW, Schenk G Chembiochem. 2019 Feb 4. doi: 10.1002/cbic.201900077. PMID:30719821[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Feder D, Gahan LR, McGeary RP, Guddat LW, Schenk G. The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State. Chembiochem. 2019 Feb 4. doi: 10.1002/cbic.201900077. PMID:30719821 doi:http://dx.doi.org/10.1002/cbic.201900077