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1fdy
From Proteopedia
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|PDB= 1fdy |SIZE=350|CAPTION= <scene name='initialview01'>1fdy</scene>, resolution 2.45Å | |PDB= 1fdy |SIZE=350|CAPTION= <scene name='initialview01'>1fdy</scene>, resolution 2.45Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=3PY:3-HYDROXYPYRUVIC ACID'>3PY</scene> | + | |LIGAND= <scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] </span> |
|GENE= NPL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= NPL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdy OCA], [http://www.ebi.ac.uk/pdbsum/1fdy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fdy RCSB]</span> | ||
}} | }} | ||
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[[Category: Pilling, P A.]] | [[Category: Pilling, P A.]] | ||
[[Category: Smith, B J.]] | [[Category: Smith, B J.]] | ||
| - | [[Category: 3PY]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
[[Category: alpha-keto-acid lyase]] | [[Category: alpha-keto-acid lyase]] | ||
| Line 37: | Line 39: | ||
[[Category: oxo-acid lyase]] | [[Category: oxo-acid lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:21:01 2008'' |
Revision as of 17:21, 30 March 2008
| |||||||
| , resolution 2.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | NPL (Escherichia coli) | ||||||
| Activity: | N-acetylneuraminate lyase, with EC number 4.1.3.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1FDY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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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