2uzz | pdb_00002uzz

X-ray structure of N-methyl-L-tryptophan oxidase (MTOX)

spinqualitylabelsall models 2uzz, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2uzz is a 4 chain structure with sequence from Ecobd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MTOX_ECOLI] Catalyzes the oxidative demethylation of N-methyl-L-tryptophan. Can also use other N-methyl amino acids, including sarcosine, which, however, is a poor substrate.[HAMAP-Rule:MF_00515] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The X-ray structure of monomeric N-methyltryptophan oxidase from Escherichia coli (MTOX) has been solved at 3.2 A resolution by molecular replacement methods using Bacillus sp. sarcosine oxidase structure (MSOX, 43% sequence identity) as search model. The analysis of the substrate binding site highlights the structural determinants that favour the accommodation of the bulky N-methyltryptophan residue in MTOX. In fact, although the nature and geometry of the catalytic residues within the first contact shell of the FAD moiety appear to be virtually superposable in MTOX and MSOX, the presence of a Thr residue in position 239 in MTOX (Met245 in MSOX) located at the entrance of the active site appears to play a key role for the recognition of the amino acid substrate side chain. Accordingly, a 15 fold increase in k(cat) and 100 fold decrease in K(m) for sarcosine as substrate has been achieved in MTOX upon T239M mutation, with a concomitant three-fold decrease in activity towards N-methyltryptophan. These data provide clear evidence for the presence of a catalytic core, common to the members of the methylaminoacid oxidase subfamily, and of a side chain recognition pocket, located at the entrance of the active site, that can be adjusted to host diverse aminoacids in the different enzyme species. The site involved in the covalent attachment of flavin has also been addressed by screening degenerate mutants in the relevant positions around Cys308-FAD linkage. Lys341 appears to be the key residue involved in flavin incorporation and covalent linkage. Proteins 2008. (c) 2008 Wiley-Liss, Inc. The X-ray structure of N-methyltryptophan oxidase reveals the structural determinants of substrate specificity.,Ilari A, Bonamore A, Franceschini S, Fiorillo A, Boffi A, Colotti G Proteins. 2008 Jan 10;. PMID:18186483 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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