1fdy: Difference between revisions

Revision as of 03:06, 1 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:1fdy.png

Template:STRUCTURE 1fdy

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATEN-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE

Template:ABSTRACT PUBMED 9047371

About this StructureAbout this Structure

1FDY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase., Lawrence MC, Barbosa JA, Smith BJ, Hall NE, Pilling PA, Ooi HC, Marcuccio SM, J Mol Biol. 1997 Feb 21;266(2):381-99. PMID:9047371

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OCA

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-'''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE'''
+===N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE===
-==Overview==
+<!--
-We describe here a sub-family of enzymes related both structurally and functionally to N-acetylneuraminate lyase. Two members of this family (N-acetylneuraminate lyase and dihydrodipicolinate synthase) have known three-dimensional structures and we now proceed to show their structural and functional relationship to two further proteins, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase and D-4-deoxy-5-oxoglucarate dehydratase. These enzymes are all thought to involve intermediate Schiff-base formation with their respective substrates. In order to understand the nature of this intermediate, we have determined the three-dimensional structure of N-acetylneuraminate lyase in complex with hydroxypyruvate (a product analogue) and in complex with one of its products (pyruvate). From these structures we deduce the presence of a closely similar Schiff-base forming motif in all members of the N-acetylneuraminate lyase sub-family. A fifth protein, MosA, is also confirmed to be a member of the sub-family although the involvement of an intermediate Schiff-base in its proposed reaction is unclear.
+The line below this paragraph, {{ABSTRACT_PUBMED_9047371}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9047371}}
 ==About this Structure==
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 [[Category: Lyase]]
 [[Category: Oxo-acid lyase]]
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