1knr: Difference between revisions
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[[Image:1knr.gif|left|200px]] | [[Image:1knr.gif|left|200px]] | ||
'''L-aspartate oxidase: R386L mutant''' | {{Structure | ||
|PDB= 1knr |SIZE=350|CAPTION= <scene name='initialview01'>1knr</scene>, resolution 2.500Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/L-aspartate_oxidase L-aspartate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.16 1.4.3.16] | |||
|GENE= NADB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''L-aspartate oxidase: R386L mutant''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KNR is a [ | 1KNR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNR OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11863440 11863440] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: L-aspartate oxidase]] | [[Category: L-aspartate oxidase]] | ||
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[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: NA]] | [[Category: NA]] | ||
[[Category: fumarate reductase family of | [[Category: fumarate reductase family of oxidoreductase]] | ||
[[Category: succinate dehydrogenase]] | [[Category: succinate dehydrogenase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:51 2008'' | ||
Revision as of 10:19, 20 March 2008
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| 1knr, resolution 2.500Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CL, NA and FAD | ||||||||||||
| Gene: | NADB (Escherichia coli) | ||||||||||||
| Activity: | L-aspartate oxidase, with EC number 1.4.3.16 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
L-aspartate oxidase: R386L mutant
Overview
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.
About this Structure
1KNR 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
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