1s5o: Difference between revisions

Revision as of 12:09, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1s5o.png

Template:STRUCTURE 1s5o

Structural and Mutational Characterization of L-carnitine Binding to Human carnitine AcetyltransferaseStructural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase

Template:ABSTRACT PUBMED 15099582

About this StructureAbout this Structure

1S5O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase., Govindasamy L, Kukar T, Lian W, Pedersen B, Gu Y, Agbandje-McKenna M, Jin S, McKenna R, Wu D, J Struct Biol. 2004 Jun;146(3):416-24. PMID:15099582

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''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==
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-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
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 [[Category: Substrate binding site]]
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