2byd: Difference between revisions

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-[[Image:2byd.gif|left|200px]]
- {{Structure
+==Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase==
-|PDB= 2byd |SIZE=350|CAPTION= <scene name='initialview01'>2byd</scene>, resolution 2.00&Aring;
+<StructureSection load='2byd' size='340' side='right'caption='[[2byd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:Br+Binding+Site+For+Chain+A'>AC1</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=BR:BROMIDE ION'>BR</scene>
+<table><tr><td colspan='2'>[[2byd]] is a 1 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=2BYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BYD FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31]
+</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>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2byd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2byd OCA], [https://pdbe.org/2byd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2byd RCSB], [https://www.ebi.ac.uk/pdbsum/2byd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2byd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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>
+== 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/by/2byd_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=2byd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-BYD 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=2BYD OCA].
+<div class="pdbe-citations 2byd" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: L-aminoadipate-semialdehyde dehydrogenase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Arrowsmith C]]
-[[Category: Arrowsmith, C.]]
+[[Category: Bunkoczi G]]
-[[Category: Bunkoczi, G.]]
+[[Category: Dubinina E]]
-[[Category: Delft, F Von.]]
+[[Category: Edwards A]]
-[[Category: Dubinina, E.]]
+[[Category: Johansson C]]
-[[Category: Edwards, A.]]
+[[Category: Oppermann U]]
-[[Category: Johansson, C.]]
+[[Category: Smee C]]
-[[Category: Oppermann, U.]]
+[[Category: Sundstrom M]]
-[[Category: Smee, C.]]
+[[Category: Turnbull A]]
-[[Category: Sundstrom, M.]]
+[[Category: Weigelt J]]
-[[Category: Turnbull, A.]]
+[[Category: Wu X]]
-[[Category: Weigelt, J.]]
+[[Category: Von Delft F]]
-[[Category: Wu, X.]]
-[[Category: BR]]
-[[Category: fatty acid biosynthesis]]
-[[Category: phosphopantetheine transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:08:23 2008''