1s5o

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[[Image:1s5o.gif|left|200px]]<br /><applet load="1s5o" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s5o.gif|left|200px]]
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caption="1s5o, resolution 1.8&Aring;" />
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'''Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase'''<br />
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{{Structure
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|PDB= 1s5o |SIZE=350|CAPTION= <scene name='initialview01'>1s5o</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=152:CARNITINE'>152</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7]
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|GENE=
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}}
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'''Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1S5O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=152:'>152</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5O OCA].
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1S5O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5O OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15099582 15099582]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15099582 15099582]
[[Category: Carnitine O-acetyltransferase]]
[[Category: Carnitine O-acetyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: binary complex]]
[[Category: binary complex]]
[[Category: carnitine acetyltransferase]]
[[Category: carnitine acetyltransferase]]
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[[Category: steady-state enzyme kinetics]]
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[[Category: steady-state enzyme kinetic]]
[[Category: substrate binding site]]
[[Category: substrate binding site]]
[[Category: x-ray structure]]
[[Category: x-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:00:49 2008''

Revision as of 12:00, 20 March 2008

Image:1s5o.gif


PDB ID 1s5o

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
Activity: Carnitine O-acetyltransferase, with EC number 2.3.1.7
Coordinates: save as pdb, mmCIF, xml



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


Contents

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.

Disease

Known disease associated with this structure: Carnitine acetyltransferase deficiency (1) OMIM:[600184]

About this Structure

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

Reference

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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