2cg5

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[[Image:2cg5.png|left|200px]]
 
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{{STRUCTURE_2cg5| PDB=2cg5 | SCENE= }}
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==Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase in complex with cytosolic acyl carrier protein and coenzyme A==
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<StructureSection load='2cg5' size='340' side='right'caption='[[2cg5]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cg5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CG5 FirstGlance]. <br>
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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]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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=2cg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cg5 OCA], [https://pdbe.org/2cg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cg5 RCSB], [https://www.ebi.ac.uk/pdbsum/2cg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cg5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADPPT_HUMAN ADPPT_HUMAN] Catalyzes the post-translational modification of target proteins by phosphopantetheine. Can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN.<ref>PMID:11286508</ref> <ref>PMID:12815048</ref> <ref>PMID:18022563</ref>
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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/cg/2cg5_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=2cg5 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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Mammals utilize a single phosphopantetheinyl transferase for the posttranslational modification of at least three different apoproteins: the carrier protein components of cytosolic and mitochondrial fatty acid synthases and the aminoadipate semialdehyde reductase involved in lysine degradation. We determined the crystal structure of the human phosphopantetheinyl transferase, a eukaryotic phosphopantetheinyl transferase characterized, complexed with CoA and Mg(2+), and in ternary complex with CoA and ACP. The involvement of key residues in ligand binding and catalysis was confirmed by mutagenesis and kinetic analysis. Human phosphopantetheinyl transferase exhibits an alpha/beta fold and 2-fold pseudosymmetry similar to the Sfp phosphopantetheinyl transferase from Bacillus subtilis. Although the bound ACP exhibits a typical four-helix structure, its binding is unusual in that it is facilitated predominantly by hydrophobic interactions. A detailed mechanism is proposed describing the substrate binding and catalytic process.
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===STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH CYTOSOLIC ACYL CARRIER PROTEIN AND COENZYME A===
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Mechanism and substrate recognition of human holo ACP synthase.,Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U Chem Biol. 2007 Nov;14(11):1243-53. PMID:18022563<ref>PMID:18022563</ref>
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{{ABSTRACT_PUBMED_18022563}}
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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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==About this Structure==
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<div class="pdbe-citations 2cg5" style="background-color:#fffaf0;"></div>
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[[2cg5]] is a 2 chain structure with 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=2CG5 OCA].
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==See Also==
==See Also==
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*[[Fatty acid synthase|Fatty acid synthase]]
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*[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:018022563</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: L-aminoadipate-semialdehyde dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C.]]
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[[Category: Arrowsmith C]]
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[[Category: Bunkoczi, G.]]
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[[Category: Bunkoczi G]]
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[[Category: Delft, F Von.]]
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[[Category: Edwards A]]
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[[Category: Edwards, A.]]
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[[Category: Joshi A]]
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[[Category: Joshi, A.]]
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[[Category: Oppermann U]]
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[[Category: Oppermann, U.]]
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[[Category: Papagrigoriu E]]
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[[Category: Papagrigoriu, E.]]
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[[Category: Smith S]]
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[[Category: Smith, S.]]
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[[Category: Sundstrom M]]
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[[Category: Sundstrom, M.]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J.]]
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[[Category: Von Delft F]]
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[[Category: Acp]]
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[[Category: Coenzyme some]]
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[[Category: Complex]]
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[[Category: Fasn]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Hydrolase]]
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[[Category: Lipid synthesis]]
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[[Category: Lyase]]
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[[Category: Phosphopantetheine transferase]]
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[[Category: Transferase]]
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[[Category: Transferase-hydrolase complex]]
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Current revision

Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase in complex with cytosolic acyl carrier protein and coenzyme A

PDB ID 2cg5

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OCA

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