2qa1

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[[Image:2qa1.gif|left|200px]]
 
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==Crystal structure of PgaE, an aromatic hydroxylase involved in angucycline biosynthesis==
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The line below this paragraph, containing "STRUCTURE_2qa1", creates the "Structure Box" on the page.
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<StructureSection load='2qa1' size='340' side='right'caption='[[2qa1]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2qa1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._PGA64 Streptomyces sp. PGA64]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QA1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QA1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2qa1| PDB=2qa1 | SCENE= }}
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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=2qa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qa1 OCA], [https://pdbe.org/2qa1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qa1 RCSB], [https://www.ebi.ac.uk/pdbsum/2qa1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qa1 ProSAT]</span></td></tr>
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</table>
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'''Crystal structure of PgaE, an aromatic hydroxylase involved in angucycline biosynthesis'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q93LY7_9ACTN Q93LY7_9ACTN]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Angucyclines are aromatic polyketides produced in Streptomycetes via complex enzymatic biosynthetic pathways. PgaE and CabE from S. sp PGA64 and S. sp. H021 are two related homo-dimeric FAD and NADPH dependent aromatic hydroxylases involved in the early steps of the angucycline core modification. Here we report the three-dimensional structures of these two enzymes determined by X-ray crystallography using multiple anomalous diffraction and molecular replacement, respectively, to resolutions of 1.8 A and 2.7 A. The enzyme subunits are built up of three domains, a FAD binding domain, a domain involved in substrate binding and a C-terminal thioredoxin-like domain of unknown function. The structure analysis identifies PgaE and CabE as members of the para-hydroxybenzoate hydroxylase (pHBH) fold family of aromatic hydroxylases. In contrast to phenol hydroxylase and 3-hydroxybenzoate hydroxylase that utilize the C-terminal domain for dimer formation, this domain is not part of the subunit-subunit interface in PgaE and CabE. Instead, dimer assembly occurs through interactions of their FAD binding domains. FAD is bound non-covalently in the "in"-conformation. The active sites in the two enzymes differ significantly from those of other aromatic hydroxylases. The volumes of the active site are significantly larger, as expected in view of the voluminous tetracyclic angucycline substrates. The structures further suggest that substrate binding and catalysis may involve dynamic rearrangements of the middle domain relative to the other two domains. Site-directed mutagenesis studies of putative catalytic groups in the active site of PgaE argue against enzyme-catalyzed substrate deprotonation as a step in catalysis. This is in contrast to pHBH, where deprotonation/protonation of the substrate has been suggested as an essential part of the enzymatic mechanism.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qa/2qa1_consurf.spt"</scriptWhenChecked>
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2QA1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp._pga64 Streptomyces sp. pga64]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QA1 OCA].
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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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==Reference==
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</jmolCheckbox>
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Crystal structures of two aromatic hydroxylases involved in the early tailoring steps of angucycline biosynthesis., Koskiniemi H, Metsa-Ketela M, Dobritzsch D, Kallio P, Korhonen H, Mantsala P, Schneider G, Niemi J, J Mol Biol. 2007 Sep 21;372(3):633-48. Epub 2007 Jul 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17669423 17669423]
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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=2qa1 ConSurf].
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[[Category: Single protein]]
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<div style="clear:both"></div>
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[[Category: Streptomyces sp. pga64]]
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__TOC__
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[[Category: Dobritzsch, D.]]
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</StructureSection>
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[[Category: Kallio, P.]]
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[[Category: Large Structures]]
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[[Category: Koskiniemi, H.]]
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[[Category: Streptomyces sp. PGA64]]
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[[Category: Metsa-Ketela, M.]]
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[[Category: Dobritzsch D]]
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[[Category: Niemi, J.]]
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[[Category: Kallio P]]
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[[Category: Schneider, G.]]
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[[Category: Koskiniemi H]]
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[[Category: Angucycline]]
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[[Category: Metsa-Ketela M]]
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[[Category: Aromatic hydroxylase]]
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[[Category: Niemi J]]
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[[Category: Fad]]
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[[Category: Schneider G]]
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[[Category: Oxidoreductase]]
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[[Category: Polyketide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:36:35 2008''
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Current revision

Crystal structure of PgaE, an aromatic hydroxylase involved in angucycline biosynthesis

PDB ID 2qa1

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