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2byd

From Proteopedia

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Current revision

Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase

Structural highlights

2byd is a 1 chain structure with sequence from Homo sapiens. 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

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.^[1] ^[2] ^[3]

Evolutionary Conservation

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

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Praphanphoj V, Sacksteder KA, Gould SJ, Thomas GH, Geraghty MT. Identification of the alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene. Mol Genet Metab. 2001 Apr;72(4):336-42. PMID:11286508 doi:http://dx.doi.org/10.1006/mgme.2000.3138
↑ Joshi AK, Zhang L, Rangan VS, Smith S. Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity. J Biol Chem. 2003 Aug 29;278(35):33142-9. Epub 2003 Jun 18. PMID:12815048 doi:http://dx.doi.org/10.1074/jbc.M305459200
↑ Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U. Mechanism and substrate recognition of human holo ACP synthase. Chem Biol. 2007 Nov;14(11):1243-53. PMID:18022563 doi:10.1016/j.chembiol.2007.10.013
↑ Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U. Mechanism and substrate recognition of human holo ACP synthase. Chem Biol. 2007 Nov;14(11):1243-53. PMID:18022563 doi:10.1016/j.chembiol.2007.10.013

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2byd"

@@ Line 3: / Line 3: @@
 <StructureSection load='2byd' size='340' side='right'caption='[[2byd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2byd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
+<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>
-</td></tr><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>
+</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-aminoadipate-semialdehyde_dehydrogenase L-aminoadipate-semialdehyde dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.31 1.2.1.31] </span></td></tr>
+<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]]
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: L-aminoadipate-semialdehyde dehydrogenase]]
 [[Category: Large Structures]]
-[[Category: Arrowsmith, C]]
+[[Category: Arrowsmith C]]
-[[Category: Bunkoczi, G]]
+[[Category: Bunkoczi G]]
-[[Category: Delft, F von]]
+[[Category: Dubinina E]]
-[[Category: Dubinina, E]]
+[[Category: Edwards A]]
-[[Category: Edwards, A]]
+[[Category: Johansson C]]
-[[Category: Johansson, C]]
+[[Category: Oppermann U]]
-[[Category: Oppermann, U]]
+[[Category: Smee C]]
-[[Category: Smee, C]]
+[[Category: Sundstrom M]]
-[[Category: Sundstrom, M]]
+[[Category: Turnbull A]]
-[[Category: Turnbull, A]]
+[[Category: Weigelt J]]
-[[Category: Weigelt, J]]
+[[Category: Wu X]]
-[[Category: Wu, X]]
+[[Category: Von Delft F]]
-[[Category: Fatty acid biosynthesis]]
-[[Category: Phosphopantetheine transferase]]
-[[Category: Transferase]]

2byd

From Proteopedia

Current revision

Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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