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| - | [[Image:1knp.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1knp| PDB=1knp | SCENE= }} | | {{STRUCTURE_1knp| PDB=1knp | SCENE= }} |
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| - | '''E. coli L-aspartate oxidase: mutant R386L in complex with succinate'''
| + | ===E. coli L-aspartate oxidase: mutant R386L in complex with succinate=== |
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| - | ==Overview==
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| - | L-Aspartate oxidase (Laspo) catalyzes the conversion of L-Asp to iminoaspartate, the first step in the de novo biosynthesis of NAD(+). This bacterial pathway represents a potential drug target since it is absent in mammals. The Laspo R386L mutant was crystallized in the FAD-bound catalytically competent form and its three-dimensional structure determined at 2.5 A resolution in both the native state and in complex with succinate. Comparison of the R386L holoprotein with the wild-type apoenzyme [Mattevi, A., Tedeschi, G., Bacchella, L., Coda, A., Negri, A., and Ronchi, S. (1999) Structure 7, 745-756] reveals that cofactor incorporation leads to the ordering of two polypeptide segments (residues 44-53 and 104-141) and to a 27 degree rotation of the capping domain. This motion results in the formation of the active site cavity, located at the interface between the capping domain and the FAD-binding domain. The structure of the succinate complex indicates that the cavity surface is decorated by two clusters of H-bond donors that anchor the ligand carboxylates. Moreover, Glu121, which is strictly conserved among Laspo sequences, is positioned to interact with the L-Asp alpha-amino group. The architecture of the active site of the Laspo holoenzyme is remarkably similar to that of respiratory fumarate reductases, providing strong evidence for a common mechanism of catalysis in Laspo and flavoproteins of the succinate dehydrogenase/fumarate reductase family. This implies that Laspo is mechanistically distinct from other flavin-dependent amino acid oxidases, such as the prototypical D-amino acid oxidase.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11863440}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11863440 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11863440}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mattevi, A.]] | | [[Category: Mattevi, A.]] |
| | [[Category: Fumarate reductase family of oxidoreductase]] | | [[Category: Fumarate reductase family of oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:57:28 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:36:26 2008'' |
Revision as of 07:36, 2 July 2008
Template:STRUCTURE 1knp
E. coli L-aspartate oxidase: mutant R386L in complex with succinate
Template:ABSTRACT PUBMED 11863440
About this Structure
1KNP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of FAD-bound L-aspartate oxidase: insight into substrate specificity and catalysis., Bossi RT, Negri A, Tedeschi G, Mattevi A, Biochemistry. 2002 Mar 5;41(9):3018-24. PMID:11863440
Page seeded by OCA on Wed Jul 2 10:36:26 2008
