4kbp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:4kbp.jpg|left|200px]] | [[Image:4kbp.jpg|left|200px]] | ||
'''KIDNEY BEAN PURPLE ACID PHOSPHATASE''' | {{Structure | ||
|PDB= 4kbp |SIZE=350|CAPTION= <scene name='initialview01'>4kbp</scene>, resolution 2.7Å | |||
|SITE= <scene name='pdbsite=ACA:Phosphatase+Active+Site'>ACA</scene>, <scene name='pdbsite=ACB:Phosphatase+Active+Site'>ACB</scene>, <scene name='pdbsite=ACC:Phosphatase+Active+Site'>ACC</scene> and <scene name='pdbsite=ACD:Phosphatase+Active+Site'>ACD</scene> | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] | |||
|GENE= | |||
}} | |||
'''KIDNEY BEAN PURPLE ACID PHOSPHATASE''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
4KBP is a [ | 4KBP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KBP OCA]. | ||
==Reference== | ==Reference== | ||
Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures., Klabunde T, Strater N, Frohlich R, Witzel H, Krebs B, J Mol Biol. 1996 Jun 21;259(4):737-48. PMID:[http:// | Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures., Klabunde T, Strater N, Frohlich R, Witzel H, Krebs B, J Mol Biol. 1996 Jun 21;259(4):737-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8683579 8683579] | ||
[[Category: Acid phosphatase]] | [[Category: Acid phosphatase]] | ||
[[Category: Phaseolus vulgaris]] | [[Category: Phaseolus vulgaris]] | ||
| Line 24: | Line 33: | ||
[[Category: purple acid phosphatase]] | [[Category: purple acid phosphatase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:05 2008'' | ||
Revision as of 20:10, 20 March 2008
| |||||||
| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , and | ||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
KIDNEY BEAN PURPLE ACID PHOSPHATASE
OverviewOverview
Purple acid phosphatase is a widely distributed non-specific phosphomonoesterase. X-ray structures of the dimeric 111-kDa Fe(III)-Zn(II) kidney bean purple acid phosphatase (kbPAP) complexed with phosphate, the product of the reaction, and with tungstate, a strong inhibitor of the phosphatase activity, were determined at 2.7 and 3.0 angstroms resolution, respectively. Furthermore the resolution of the unligated enzyme, recently solved at 2.9 angstroms could be extended to 2.65 angstroms with completely new data. The binding of both oxoanions is not accompanied by larger conformational changes in the enzyme structure. Small movements with a maximal coordinate shift of 1 angstroms are only observed for the active site residues His295 and His296. In the inhibitor complex as well as in the product complex, the oxoanion binds in a bidentate bridging mode to the two metal ions, replacing two of the presumed solvent ligands present in the unligated enzyme form. As also proposed for the unligated structure a bridging hydroxide ion completes the coordination spheres of both metal ions to octahedral arrangements. All three structures reported herein support a mechanism of phosphate ester hydrolysis involving interaction of the substrate with Zn(II) followed by a nucleophilic attack on the phosphorus by an Fe(III)-coordinated hydroxide ion. The negative charge evolving at the pentacoordinated transition state is probably stabilized by interactions with the divalent zinc and the imidazole groups of His202, His295, and His296, the latter protonating the leaving alcohol group.
About this StructureAbout this Structure
4KBP is a Single protein structure of sequence from Phaseolus vulgaris. Full crystallographic information is available from OCA.
ReferenceReference
Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures., Klabunde T, Strater N, Frohlich R, Witzel H, Krebs B, J Mol Biol. 1996 Jun 21;259(4):737-48. PMID:8683579
Page seeded by OCA on Thu Mar 20 19:10:05 2008