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.


1fdy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fdy.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fdy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fdy| PDB=1fdy | SCENE= }}
{{STRUCTURE_1fdy| PDB=1fdy | SCENE= }}
-
'''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
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9047371 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9047371}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Oxo-acid lyase]]
[[Category: Oxo-acid lyase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:12:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:06:41 2008''

Revision as of 00:06, 1 July 2008

Template:STRUCTURE 1fdy

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE

Template:ABSTRACT PUBMED 9047371

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

Page seeded by OCA on Tue Jul 1 03:06:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools