1knp
From Proteopedia
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|PDB= 1knp |SIZE=350|CAPTION= <scene name='initialview01'>1knp</scene>, resolution 2.600Å | |PDB= 1knp |SIZE=350|CAPTION= <scene name='initialview01'>1knp</scene>, resolution 2.600Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= NADB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= NADB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1chu|1CHU]], [[1knr|1KNR]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1knp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1knp OCA], [http://www.ebi.ac.uk/pdbsum/1knp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1knp RCSB]</span> | ||
}} | }} | ||
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[[Category: Bossi, R T.]] | [[Category: Bossi, R T.]] | ||
[[Category: Mattevi, A.]] | [[Category: Mattevi, A.]] | ||
| - | [[Category: FAD]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: SIN]] | ||
[[Category: fumarate reductase family of oxidoreductase]] | [[Category: fumarate reductase family of oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:01 2008'' |
Revision as of 18:51, 30 March 2008
| |||||||
| , resolution 2.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | NADB (Escherichia coli) | ||||||
| Activity: | L-aspartate oxidase, with EC number 1.4.3.16 | ||||||
| Related: | 1CHU, 1KNR
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E. coli L-aspartate oxidase: mutant R386L in complex with succinate
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
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
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