2rcu

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[[Image:2rcu.gif|left|200px]]
 
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{{Structure
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==Crystal structure of rat carnitine palmitoyltransferase 2 in complex with r-3-(hexadecanoylamino)-4-(trimethylazaniumyl)butanoate==
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|PDB= 2rcu |SIZE=350|CAPTION= <scene name='initialview01'>2rcu</scene>, resolution 1.78&Aring;
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<StructureSection load='2rcu' size='340' side='right'caption='[[2rcu]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=BUJ:(3R)-3-(HEXADECANOYLAMINO)-4-(TRIMETHYLAMMONIO)BUTANOATE'>BUJ</scene>
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<table><tr><td colspan='2'>[[2rcu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RCU FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carnitine_O-palmitoyltransferase Carnitine O-palmitoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.21 2.3.1.21] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
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|GENE= Cpt2, Cpt-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=BUJ:(3R)-3-(HEXADECANOYLAMINO)-4-(TRIMETHYLAMMONIO)BUTANOATE'>BUJ</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcu OCA], [https://pdbe.org/2rcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rcu RCSB], [https://www.ebi.ac.uk/pdbsum/2rcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rcu ProSAT]</span></td></tr>
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|RELATEDENTRY=[[2deb|2DEB]], [[2fw3|2FW3]], [[2fyo|2FYO]], [[2h4t|2H4T]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rcu OCA], [http://www.ebi.ac.uk/pdbsum/2rcu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rcu RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/CPT2_RAT CPT2_RAT]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rc/2rcu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2rcu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mitochondrial membrane-associated carnitine palmitoyltransferase system is a validated target for the treatment of type 2 diabetes mellitus. To further facilitate structure-based drug discovery, we determined the crystal structure of rat CPT-2 (rCPT-2) in complex with the substrate analogue palmitoyl-aminocarnitine at 1.8A resolution. Biochemical analyses revealed a strong effect of this compound on rCPT-2 activity and stability. Using a computational approach we examined the membrane association of rCPT-2. The protein interacts with the membrane as a functional monomer and the calculations confirm the presence of a membrane association domain that consists of layers of hydrophobic and positively charged residues.
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'''Crystal structure of rat carnitine palmitoyltransferase 2 in complex with r-3-(hexadecanoylamino)-4-(trimethylazaniumyl)butanoate'''
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Carnitine palmitoyltransferase 2: analysis of membrane association and complex structure with a substrate analog.,Rufer AC, Lomize A, Benz J, Chomienne O, Thoma R, Hennig M FEBS Lett. 2007 Jul 10;581(17):3247-52. Epub 2007 Jun 8. PMID:17585909<ref>PMID:17585909</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2rcu" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The mitochondrial membrane-associated carnitine palmitoyltransferase system is a validated target for the treatment of type 2 diabetes mellitus. To further facilitate structure-based drug discovery, we determined the crystal structure of rat CPT-2 (rCPT-2) in complex with the substrate analogue palmitoyl-aminocarnitine at 1.8A resolution. Biochemical analyses revealed a strong effect of this compound on rCPT-2 activity and stability. Using a computational approach we examined the membrane association of rCPT-2. The protein interacts with the membrane as a functional monomer and the calculations confirm the presence of a membrane association domain that consists of layers of hydrophobic and positively charged residues.
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*[[Carnitine palmitoyltransferase|Carnitine palmitoyltransferase]]
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== References ==
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==About this Structure==
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<references/>
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2RCU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCU OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Carnitine palmitoyltransferase 2: analysis of membrane association and complex structure with a substrate analog., Rufer AC, Lomize A, Benz J, Chomienne O, Thoma R, Hennig M, FEBS Lett. 2007 Jul 10;581(17):3247-52. Epub 2007 Jun 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17585909 17585909]
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[[Category: Carnitine O-palmitoyltransferase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Benz J]]
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[[Category: Benz, J.]]
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[[Category: Chomienne O]]
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[[Category: Chomienne, O.]]
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[[Category: Hennig M]]
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[[Category: Hennig, M.]]
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[[Category: Rufer AC]]
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[[Category: Rufer, A C.]]
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[[Category: Thoma R]]
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[[Category: Thoma, R.]]
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[[Category: acetylation]]
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[[Category: acyltransferase]]
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[[Category: fatty acid metabolism]]
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[[Category: inner membrane]]
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[[Category: lipid metabolism]]
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[[Category: membrane]]
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[[Category: mitochondrial protein]]
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[[Category: mitochondrion]]
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[[Category: transferase]]
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[[Category: transferase 04-mai-06 r]]
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[[Category: transit peptide]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:58:56 2008''
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Current revision

Crystal structure of rat carnitine palmitoyltransferase 2 in complex with r-3-(hexadecanoylamino)-4-(trimethylazaniumyl)butanoate

PDB ID 2rcu

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