This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1fdz
From Proteopedia
(New page: 200px<br /><applet load="1fdz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fdz, resolution 2.6Å" /> '''N-ACETYLNEURAMINATE L...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1fdz.gif|left|200px]]<br /><applet load="1fdz" size=" | + | [[Image:1fdz.gif|left|200px]]<br /><applet load="1fdz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fdz, resolution 2.6Å" /> | caption="1fdz, resolution 2.6Å" /> | ||
'''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION'''<br /> | '''N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION'''<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== | ||
| - | 1FDZ 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 PYR 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:// | + | 1FDZ 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=PYR:'>PYR</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=1FDZ OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[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: PYR]] | [[Category: PYR]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
| Line 28: | Line 28: | ||
[[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 12:37:41 2008'' |
Revision as of 10:37, 21 February 2008
|
N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH PYRUVATE VIA BOROHYDRIDE REDUCTION
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
1FDZ 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
Page seeded by OCA on Thu Feb 21 12:37:41 2008
