This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2dyu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2dyu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2dyu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2dyu| PDB=2dyu | SCENE= }}
{{STRUCTURE_2dyu| PDB=2dyu | 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==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17307742}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17307742 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17307742}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 4 09:57:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:58:16 2008''

Revision as of 21:58, 27 July 2008

Image:2dyu.png

Template:STRUCTURE 2dyu

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

Template:ABSTRACT PUBMED 17307742

About this Structure

2DYU is a Single protein structure of sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA.

Reference

Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad., Hung CL, Liu JH, Chiu WC, Huang SW, Hwang JK, Wang WC, J Biol Chem. 2007 Apr 20;282(16):12220-9. Epub 2007 Feb 16. PMID:17307742

Page seeded by OCA on Mon Jul 28 00:58:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dyu"
Personal tools