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| - | [[Image:2plk.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2plk| PDB=2plk | SCENE= }} | | {{STRUCTURE_2plk| PDB=2plk | SCENE= }} |
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| - | '''Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from Vibrio vulnificus'''
| + | ===Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from Vibrio vulnificus=== |
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| - | ==Overview==
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| - | The beta/alpha-barrel fold type basic amino acid decarboxylases include eukaryotic ornithine decarboxylases (ODC) and bacterial and plant enzymes with activity on L-arginine and meso-diaminopimelate. These enzymes catalyze essential steps in polyamine and lysine biosynthesis. Phylogenetic analysis suggests that diverse bacterial species also contain ODC-like enzymes from this fold type. However, in comparison with the eukaryotic ODCs, amino acid differences were identified in the sequence of the 3(10)-helix that forms a key specificity element in the active site, suggesting they might function on novel substrates. Putative decarboxylases from a phylogenetically diverse range of bacteria were characterized to determine their substrate preference. Enzymes from species within Methanosarcina, Pseudomonas, Bartonella, Nitrosomonas, Thermotoga, and Aquifex showed a strong preference for L-ornithine, whereas the enzyme from Vibrio vulnificus (VvL/ODC) had dual specificity functioning well on both L-ornithine and L-lysine. The x-ray structure of VvL/ODC was solved in the presence of the reaction products putrescine and cadaverine to 1.7 and 2.15A, respectively. The overall structure is similar to eukaryotic ODC; however, reorientation of the 3(10)-helix enlarging the substrate binding pocket allows L-lysine to be accommodated. The structure of the putrescine-bound enzyme suggests that a bridging water molecule between the shorter L-ornithine and key active site residues provides the structural basis for VvL/ODC to also function on this substrate. Our data demonstrate that there is greater structural and functional diversity in bacterial polyamine biosynthetic decarboxylases than previously suspected. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17626020}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17626020 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17626020}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lyase]] | | [[Category: Lyase]] |
| | [[Category: Type iv decarboxylase]] | | [[Category: Type iv decarboxylase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:22:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:26:40 2008'' |
Revision as of 19:26, 27 July 2008
Template:STRUCTURE 2plk
Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from Vibrio vulnificus
Template:ABSTRACT PUBMED 17626020
About this Structure
2PLK is a Single protein structure of sequence from Vibrio vulnificus. Full crystallographic information is available from OCA.
Reference
Phylogenetic diversity and the structural basis of substrate specificity in the beta/alpha-barrel fold basic amino acid decarboxylases., Lee J, Michael AJ, Martynowski D, Goldsmith EJ, Phillips MA, J Biol Chem. 2007 Sep 14;282(37):27115-25. Epub 2007 Jul 11. PMID:17626020
Page seeded by OCA on Sun Jul 27 22:26:40 2008
