1s5o: Difference between revisions

Revision as of 08:19, 3 May 2008

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

OverviewOverview

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.

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 Page seeded by OCA on Sat May 3 08:19:56 2008

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

OCA

@@ Line 1: / Line 1: @@
 [[Image:1s5o.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1s5o |SIZE=350|CAPTION= <scene name='initialview01'>1s5o</scene>, resolution 1.8&Aring;
+The line below this paragraph, containing "STRUCTURE_1s5o", creates the "Structure Box" on the page.
-|SITE=
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=152:CARNITINE'>152</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE=
+-->
-|DOMAIN=
+{{STRUCTURE_1s5o|  PDB=1s5o  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s5o OCA], [http://www.ebi.ac.uk/pdbsum/1s5o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s5o RCSB]</span>
-}}
 '''Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase'''
@@ Line 35: / Line 32: @@
 [[Category: Pedersen, B.]]
 [[Category: Wu, D.]]
-[[Category: binary complex]]
+[[Category: Binary complex]]
-[[Category: carnitine acetyltransferase]]
+[[Category: Carnitine acetyltransferase]]
-[[Category: steady-state enzyme kinetic]]
+[[Category: Steady-state enzyme kinetic]]
-[[Category: substrate binding site]]
+[[Category: Substrate binding site]]
-[[Category: x-ray structure]]
+[[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 Sun Mar 30 23:37:44 2008''