4fua

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[[Image:4fua.jpg|left|200px]]
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{{STRUCTURE_4fua| PDB=4fua | SCENE= }}
{{STRUCTURE_4fua| PDB=4fua | SCENE= }}
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'''L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH'''
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===L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH===
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==Overview==
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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.
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(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==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Zinc enzyme]]
[[Category: Zinc enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:24:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:37:31 2008''

Revision as of 10:37, 3 July 2008

Template:STRUCTURE 4fua

L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH

Template:ABSTRACT PUBMED 8676381

About this Structure

4FUA is a Single protein structure of sequence from Escherichia coli. 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 Jul 3 13:37:31 2008

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