3fua: Difference between revisions
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'''L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K''' | '''L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K''' | ||
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[[Category: Dreyer, M K.]] | [[Category: Dreyer, M K.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
[[Category: | [[Category: Class ii aldolase]] | ||
[[Category: | [[Category: Lyase]] | ||
[[Category: | [[Category: Zinc enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:02:04 2008'' | |||
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Revision as of 22:02, 4 May 2008
L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K
OverviewOverview
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 StructureAbout this Structure
3FUA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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 Sun May 4 22:02:04 2008