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2plj

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[[Image:2plj.jpg|left|200px]]
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{{STRUCTURE_2plj| PDB=2plj | SCENE= }}
{{STRUCTURE_2plj| PDB=2plj | SCENE= }}
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'''Crystal structure of lysine/ornithine decarboxylase complexed with putrescine from Vibrio vulnificus'''
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===Crystal structure of lysine/ornithine decarboxylase complexed with putrescine 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.
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{{ABSTRACT_PUBMED_17626020}}
==About this Structure==
==About this Structure==
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[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Type iv decarboxylase]]
[[Category: Type iv decarboxylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:21:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:52:47 2008''

Revision as of 16:52, 28 July 2008

Image:2plj.png

Template:STRUCTURE 2plj

Crystal structure of lysine/ornithine decarboxylase complexed with putrescine from Vibrio vulnificus

Template:ABSTRACT PUBMED 17626020

About this Structure

2PLJ 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

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