1fdy
From Proteopedia
(New page: 200px<br /><applet load="1fdy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fdy, resolution 2.45Å" /> '''N-ACETYLNEURAMINATE ...) |
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| - | [[Image:1fdy.gif|left|200px]]<br /><applet load="1fdy" size=" | + | [[Image:1fdy.gif|left|200px]]<br /><applet load="1fdy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fdy, resolution 2.45Å" /> | caption="1fdy, resolution 2.45Å" /> | ||
'''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE'''<br /> | '''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We describe here a sub-family of enzymes related both structurally and | + | 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== | ==About this Structure== | ||
| - | 1FDY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with 3PY as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1FDY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=3PY:'>3PY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FDY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: N-acetylneuraminate lyase]] | [[Category: N-acetylneuraminate lyase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Barbosa, J | + | [[Category: Barbosa, J A.R G.]] |
| - | [[Category: Hall, N | + | [[Category: Hall, N E.]] |
| - | [[Category: Lawrence, M | + | [[Category: Lawrence, M C.]] |
| - | [[Category: Marcuccio, S | + | [[Category: Marcuccio, S M.]] |
| - | [[Category: Ooi, H | + | [[Category: Ooi, H C.]] |
| - | [[Category: Pilling, P | + | [[Category: Pilling, P A.]] |
| - | [[Category: Smith, B | + | [[Category: Smith, B J.]] |
[[Category: 3PY]] | [[Category: 3PY]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
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[[Category: oxo-acid lyase]] | [[Category: oxo-acid lyase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:42 2008'' |
Revision as of 10:37, 21 February 2008
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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 with as ligand. Active as N-acetylneuraminate lyase, with EC number 4.1.3.3 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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