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| - | [[Image:2uzz.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2uzz| PDB=2uzz | SCENE= }} | | {{STRUCTURE_2uzz| PDB=2uzz | SCENE= }} |
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| - | '''X-RAY STRUCTURE OF N-METHYL-L-TRYPTOPHAN OXIDASE (MTOX)'''
| + | ===X-RAY STRUCTURE OF N-METHYL-L-TRYPTOPHAN OXIDASE (MTOX)=== |
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| - | ==Overview==
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| - | 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 line below this paragraph, {{ABSTRACT_PUBMED_18186483}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18186483 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18186483}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Oxidative demethylation of n-methyl-l-tryptophan]] | | [[Category: Oxidative demethylation of n-methyl-l-tryptophan]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:55:36 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:58:45 2008'' |
Revision as of 07:58, 29 July 2008
Template:STRUCTURE 2uzz
X-RAY STRUCTURE OF N-METHYL-L-TRYPTOPHAN OXIDASE (MTOX)
Template:ABSTRACT PUBMED 18186483
About this Structure
2UZZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Jul 29 10:58:45 2008
