2e2k: Difference between revisions

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[[Image:2e2k.gif|left|200px]]
{{Seed}}
[[Image:2e2k.png|left|200px]]


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{{STRUCTURE_2e2k|  PDB=2e2k  |  SCENE=  }}  
{{STRUCTURE_2e2k|  PDB=2e2k  |  SCENE=  }}  


'''Helicobacter pylori formamidase AmiF contains a fine-tuned cysteine-glutamate-lysine catalytic triad'''
===Helicobacter pylori formamidase AmiF contains a fine-tuned cysteine-glutamate-lysine catalytic triad===




==Overview==
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Helicobacter pylori AmiF formamidase that hydrolyzes formamide to produce formic acid and ammonia belongs to a member of the nitrilase superfamily. The crystal structure of AmiF was solved to 1.75A resolution using single-wavelength anomalous dispersion methods. The structure consists of a homohexamer related by 3-fold symmetry in which each subunit has an alpha-beta-beta-alpha four-layer architecture characteristic of the nitrilase superfamily. One exterior alpha layer faces the solvent, whereas the other one associates with that of the neighbor subunit, forming a tight alpha-beta-beta-alpha-alpha-beta-beta-alpha dimer. The apo and liganded crystal structures of an inactive mutant C166S were also determined to 2.50 and 2.30 A, respectively. These structures reveal a small formamide-binding pocket that includes Cys(166), Glu(60), and Lys(133) catalytic residues, in which Cys(166) acts as a nucleophile. Analysis of the liganded AmiF and N-carbamoyl d-amino acid amidohydrolase binding pockets reveals a common Cys-Glu-Lys triad, another conserved glutamate, and different subsets of ligand-binding residues. Molecular dynamic simulations show that the conserved triad has minimal fluctuations, catalyzing the hydrolysis of a specific nitrile or amide in the nitrilase superfamily efficiently.
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{{ABSTRACT_PUBMED_17307742}}


==About this Structure==
==About this Structure==
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[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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