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4fua
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form | + | 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== | ||
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[[Category: L-fuculose-phosphate aldolase]] | [[Category: L-fuculose-phosphate aldolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dreyer, M | + | [[Category: Dreyer, M K.]] |
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: BME]] | [[Category: BME]] | ||
[[Category: PGH]] | [[Category: PGH]] | ||
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[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:17 2008'' |
Revision as of 17:13, 21 February 2008
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L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH
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
4FUA is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Active as L-fuculose-phosphate aldolase, with EC number 4.1.2.17 Known structural/functional Sites: and . 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 Thu Feb 21 19:13:17 2008
