1s5o: Difference between revisions

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-[[Image:1s5o.gif|left|200px]]
+{{Seed}}
+[[Image:1s5o.png|left|200px]]
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 {{STRUCTURE_1s5o|  PDB=1s5o  |  SCENE=  }}
-'''Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase'''
+===Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase===
-==Overview==
+<!--
-We report the crystal structure of a binary complex of human peroxisomal carnitine acetyltransferase and the substrate l-carnitine, refined to a resolution of 1.8 Angstrom with an R(factor) value of 18.9% (R(free)=22.3%). L-carnitine binds to a preformed pocket in the active site tunnel of carnitine acetyltransferase aligned with His(322). The quaternary nitrogen of carnitine forms a pi-cation interaction with Phe(545), while Arg(497) forms an electrostatic interaction with the negatively charged carboxylate group. An extensive hydrogen bond network also occurs between the carboxylate group and Tyr(431), Thr(444), and a bound water molecule. Site-directed mutagenesis and kinetic characterization reveals that Tyr(431), Thr(444), Arg(497), and Phe(545) are essential for high affinity binding of L-carnitine.
+The line below this paragraph, {{ABSTRACT_PUBMED_15099582}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15099582 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15099582}}
 ==About this Structure==
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 [[Category: Substrate binding site]]
 [[Category: X-ray structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:19:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:09:26 2008''