2uxy: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:2uxy.gif|left|200px]]
{{Seed}}
[[Image:2uxy.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2uxy|  PDB=2uxy  |  SCENE=  }}  
{{STRUCTURE_2uxy|  PDB=2uxy  |  SCENE=  }}  


'''ALIPHATIC AMIDASE'''
===ALIPHATIC AMIDASE===




==Overview==
<!--  
Microbial amidases belong to the thiol nitrilases family and have potential biotechnological applications in chemical and pharmaceutical industries as well as in bioremediation. The amidase from Pseudomonas aeruginosa isa6 x 38-kDa enzyme that catalyzes the hydrolysis of a small range of short aliphatic amides. The hereby reported high resolution crystallographic structure shows that each amidase monomer is formed by a globular four-layer alphabetabetaalpha sandwich domain with an additional 81-residue long C-terminal segment. This wraps arm-in-arm with a homologous C-terminal chain of another monomer, producing a strongly packed dimer. In the crystal, the biological active homo-hexameric amidase is built grouping three such dimers around a crystallographic 3-fold axis. The structure also elucidates the structural basis for the enzyme activity, with the nitrilases catalytic triad at the bottom of a 13-A deep, funnel-shaped pocket, accessible from the solvent through a narrow neck with 3-A diameter. An acyl transfer intermediate, resulting from the purification protocol, was found bound to the amidase nucleophilic agent, Cys(166). These results suggest that some pocket defining residues should undergo conformational shifts to allow substrates and products to access and leave the catalytic pocket, for turnover to occur.
The line below this paragraph, {{ABSTRACT_PUBMED_17442671}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17442671 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17442671}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Thiol enzyme]]
[[Category: Thiol enzyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:46:50 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:54:04 2008''

Revision as of 15:54, 27 July 2008

File:2uxy.png

Template:STRUCTURE 2uxy

ALIPHATIC AMIDASE

Template:ABSTRACT PUBMED 17442671

About this Structure

2UXY is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Structure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate state., Andrade J, Karmali A, Carrondo MA, Frazao C, J Biol Chem. 2007 Jul 6;282(27):19598-605. Epub 2007 Apr 17. PMID:17442671

Page seeded by OCA on Sun Jul 27 18:54:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2uxy&oldid=661736"