1ew8
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1ew8.gif|left|200px]] | [[Image:1ew8.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1ew8", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1ew8| PDB=1ew8 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''ALKALINE PHOSPHATASE (E.C. 3.1.3.1) COMPLEX WITH PHOSPHONOACETIC ACID''' | '''ALKALINE PHOSPHATASE (E.C. 3.1.3.1) COMPLEX WITH PHOSPHONOACETIC ACID''' | ||
| Line 32: | Line 29: | ||
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
[[Category: Widlanski, T S.]] | [[Category: Widlanski, T S.]] | ||
| - | [[Category: | + | [[Category: Enzyme-inhibitor complex]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:35:31 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:35, 2 May 2008
ALKALINE PHOSPHATASE (E.C. 3.1.3.1) COMPLEX WITH PHOSPHONOACETIC ACID
Overview
Two high resolution crystal structures of Escherichia coli alkaline phosphatase (AP) in the presence of phosphonate inhibitors are reported. The phosphonate compounds, phosphonoacetic acid (PAA) and mercaptomethylphosphonic acid (MMP), bind competitively to AP with dissociation constants of 5.5 and 0.6 mM, respectively. The structures of the complexes of AP with PAA and MMP were refined at high resolution to crystallographic R-values of 19.0 and 17.5%, respectively. Refinement of the AP-inhibitor complexes was carried out using X-PLOR. The final round of refinement was done using SHELXL-97. Crystallographic analyses of the inhibitor complexes reveal different binding modes for the two phosphonate compounds. The significant difference in binding constants can be attributed to these alternative binding modes observed in the high resolution X-ray structures. The phosphinyl group of PAA coordinates to the active site zinc ions in a manner similar to the competitive inhibitor and product inorganic phosphate. In contrast, MMP binds with its phosphonate moiety directed toward solvent. Both enzyme-inhibitor complexes exhibit close contacts, one of which has the chemical and geometrical potential to be considered an unconventional hydrogen bond of the type C-H...X.
About this Structure
1EW8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes., Holtz KM, Stec B, Myers JK, Antonelli SM, Widlanski TS, Kantrowitz ER, Protein Sci. 2000 May;9(5):907-15. PMID:10850800 Page seeded by OCA on Fri May 2 15:35:31 2008
