1k17: Difference between revisions

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~~{{Theoretical_model}}~~

==ALIPHATIC AMIDASE (EC 3.5.1.4)==

== Structural highlights ==

<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K17 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k17 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1k17 PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

The aliphatic amidase from Pseudomonas aeruginosa belongs to the nitrilase superfamily, and Cys(166) is the nucleophile of the catalytic mechanism. A model of amidase was built by comparative modelling using the crystal structure of the worm nitrilase-fragile histidine triad fusion protein (NitFhit; Protein Data Bank accession number 1EMS) as a template. The amidase model predicted a catalytic triad (Cys-Glu-Lys) situated at the bottom of a pocket and identical with the presumptive catalytic triad of NitFhit. Three-dimensional models for other amidases belonging to the nitrilase superfamily also predicted Cys-Glu-Lys catalytic triads. Support for the structure for the P. aeruginosa amidase came from site-direct mutagenesis and from the locations of amino acid residues that altered substrate specificity or binding when mutated.

~~[[Image~~:~~1k17~~.~~png|left|200px]]~~

Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.,Novo C, Farnaud S, Tata R, Clemente A, Brown PR Biochem J. 2002 Aug 1;365(Pt 3):731-8. PMID:11955282<ref>PMID:11955282</ref>

~~{{STRUCTURE_1k17| PDB=1k17 | SCENE= }}~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~===ALIPHATIC AMIDASE (EC 3~~.5.1.~~4)===~~

== References ==

~~{{ABSTRACT_PUBMED_11955282}}~~

__TOC__

</StructureSection>

==~~Reference~~==

<~~ref group="xtra">PMID:011955282<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Brown, P R]]

[[Category: Clemente, A]]

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@@ Line 1: / Line 1: @@
-{{Theoretical_model}}
+==ALIPHATIC AMIDASE (EC 3.5.1.4)==
+<StructureSection load='1k17' size='340' side='right' caption='[[1k17]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K17 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k17 FirstGlance], [http://www.ebi.ac.uk/pdbsum/1k17 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The aliphatic amidase from Pseudomonas aeruginosa belongs to the nitrilase superfamily, and Cys(166) is the nucleophile of the catalytic mechanism. A model of amidase was built by comparative modelling using the crystal structure of the worm nitrilase-fragile histidine triad fusion protein (NitFhit; Protein Data Bank accession number 1EMS) as a template. The amidase model predicted a catalytic triad (Cys-Glu-Lys) situated at the bottom of a pocket and identical with the presumptive catalytic triad of NitFhit. Three-dimensional models for other amidases belonging to the nitrilase superfamily also predicted Cys-Glu-Lys catalytic triads. Support for the structure for the P. aeruginosa amidase came from site-direct mutagenesis and from the locations of amino acid residues that altered substrate specificity or binding when mutated.
-[[Image:1k17.png|left|200px]]
+Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity.,Novo C, Farnaud S, Tata R, Clemente A, Brown PR Biochem J. 2002 Aug 1;365(Pt 3):731-8. PMID:11955282<ref>PMID:11955282</ref>
-{{STRUCTURE_1k17|  PDB=1k17  |  SCENE=  }}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-===ALIPHATIC AMIDASE (EC 3.5.1.4)===
+== References ==
+<references/>
-{{ABSTRACT_PUBMED_11955282}}
+__TOC__
+</StructureSection>
-==Reference==
-<ref group="xtra">PMID:011955282</ref><references group="xtra"/>
 [[Category: Brown, P R]]
 [[Category: Clemente, A]]