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3fua
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form, has been determined with and without the inhibitor, phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm), resolution, respectively. This inhibitor mimics the enediolate transition, state of the substrate moiety dihydroxyacetone phosphate. The structures, showed that dihydroxyacetone phosphate ligates the zinc ion of this, metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar, environment. At this position Glu73 accepts a proton in the initial, reaction step, producing the enediolate which is then stabilized by the, zinc ion. The other substrate moiety L-lactaldehyde was modeled, because, no binding structure . | + | The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form, has been determined with and without the inhibitor, phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm), resolution, respectively. This inhibitor mimics the enediolate transition, state of the substrate moiety dihydroxyacetone phosphate. The structures, showed that dihydroxyacetone phosphate ligates the zinc ion of this, metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar, environment. At this position Glu73 accepts a proton in the initial, reaction step, producing the enediolate which is then stabilized by the, zinc ion. The other substrate moiety L-lactaldehyde was modeled, because, no binding structure is yet available. |
==About this Structure== | ==About this Structure== | ||
| - | 3FUA is a | + | 3FUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, SO4, CL and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-fuculose-phosphate_aldolase L-fuculose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17] Structure known Active Sites: ACT and PBS. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3FUA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:55:28 2007'' |
Revision as of 12:50, 5 November 2007
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L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K
Overview
The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form, has been determined with and without the inhibitor, phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm), resolution, respectively. This inhibitor mimics the enediolate transition, state of the substrate moiety dihydroxyacetone phosphate. The structures, showed that dihydroxyacetone phosphate ligates the zinc ion of this, metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar, environment. At this position Glu73 accepts a proton in the initial, reaction step, producing the enediolate which is then stabilized by the, zinc ion. The other substrate moiety L-lactaldehyde was modeled, because, no binding structure is yet available.
About this Structure
3FUA is a Single protein structure of sequence from Escherichia coli with ZN, SO4, CL and BME as ligands. Active as L-fuculose-phosphate aldolase, with EC number 4.1.2.17 Structure known Active Sites: ACT and PBS. Full crystallographic information is available from OCA.
Reference
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure., Dreyer MK, Schulz GE, J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:8676381
Page seeded by OCA on Mon Nov 5 14:55:28 2007
Categories: Escherichia coli | L-fuculose-phosphate aldolase | Single protein | Dreyer, M.K. | Schulz, G.E. | BME | CL | SO4 | ZN | Class ii aldolase | Lyase | Zinc enzyme
