3fua: Difference between revisions

Revision as of 13:50, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3fua.png

Template:STRUCTURE 3fua

L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM KL-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K

Template:ABSTRACT PUBMED 8676381

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 Jul 27 13:50:03 2008

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OCA

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-'''L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8676381}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8676381 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8676381}}
 ==About this Structure==
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 [[Category: Lyase]]
 [[Category: Zinc enzyme]]
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