1xmc: Difference between revisions

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New page: left|200px<br /><applet load="1xmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xmc, resolution 2.00Å" /> '''C323M mutant structu...
 
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[[Image:1xmc.gif|left|200px]]<br /><applet load="1xmc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1xmc, resolution 2.00&Aring;" />
'''C323M mutant structure of mouse carnitine octanoyltransferase'''<br />


==Overview==
==C323M mutant structure of mouse carnitine octanoyltransferase==
Carnitine acyltransferases have crucial functions in fatty acid, metabolism. Members of this enzyme family show distinctive substrate, preferences for short-, medium- or long-chain fatty acids. The molecular, mechanism for this substrate selectivity is not clear as so far only the, structure of carnitine acetyltransferase has been determined. To further, our understanding of these important enzymes, we report here the crystal, structures at up to 2.0-A resolution of mouse carnitine, octanoyltransferase alone and in complex with the substrate, octanoylcarnitine. The structures reveal significant differences in the, acyl group binding pocket between carnitine octanoyltransferase and, carnitine acetyltransferase. Amino acid substitutions and structural, changes produce a larger hydrophobic pocket that binds the octanoyl group, in an extended conformation. Mutation of a single residue (Gly-553) in, this pocket can change the substrate preference between short- and, medium-chain acyl groups. The side chains of Cys-323 and Met-335 at the, bottom of this pocket assume dual conformations in the substrate complex, and mutagenesis studies suggest that the Met-335 residue is important for, catalysis.
<StructureSection load='1xmc' size='340' side='right'caption='[[1xmc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1xmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XMC FirstGlance]. <br>
1XMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with EPE and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carnitine_O-octanoyltransferase Carnitine O-octanoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.137 2.3.1.137] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XMC OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xmc OCA], [https://pdbe.org/1xmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xmc RCSB], [https://www.ebi.ac.uk/pdbsum/1xmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xmc ProSAT]</span></td></tr>
Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity., Jogl G, Hsiao YS, Tong L, J Biol Chem. 2005 Jan 7;280(1):738-44. Epub 2004 Oct 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15492013 15492013]
</table>
[[Category: Carnitine O-octanoyltransferase]]
== Function ==
[https://www.uniprot.org/uniprot/OCTC_MOUSE OCTC_MOUSE] Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xmc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xmc ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Hsiao YS]]
[[Category: Hsiao, Y.S.]]
[[Category: Jogl G]]
[[Category: Jogl, G.]]
[[Category: Tong L]]
[[Category: Tong, L.]]
[[Category: EPE]]
[[Category: MPD]]
[[Category: carnitine]]
[[Category: hepes]]
[[Category: mpd]]
[[Category: mutant]]
[[Category: octanoyltransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:10:27 2007''

Latest revision as of 11:51, 14 February 2024

C323M mutant structure of mouse carnitine octanoyltransferaseC323M mutant structure of mouse carnitine octanoyltransferase

Structural highlights

1xmc is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OCTC_MOUSE Beta-oxidation of fatty acids. The highest activity concerns the C6 to C10 chain length substrate (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1xmc, resolution 2.00Å

Drag the structure with the mouse to rotate

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

OCA
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