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2np9
From Proteopedia
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| - | [[Image:2np9.png|left|200px]] | ||
| - | + | ==Crystal structure of a dioxygenase in the Crotonase superfamily== | |
| + | <StructureSection load='2np9' size='340' side='right'caption='[[2np9]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2np9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_toyocaensis Streptomyces toyocaensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NP9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=YE1:[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXY-3-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL+(3R)-4-({3-[(2-{[(3,5-DIHYDROXYPHENYL)ACETYL]AMINO}ETHYL)AMINO]-3-OXOPROPYL}AMINO)-3-HYDROXY-2,2-DIMETHYL-4-OXOBUTYL+DIHYDROGEN+DIPHOSPHATE'>YE1</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=2np9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2np9 OCA], [https://pdbe.org/2np9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2np9 RCSB], [https://www.ebi.ac.uk/pdbsum/2np9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2np9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DPGC_STRTO DPGC_STRTO] Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the unusual conversion 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) to 3,5-dihydroxyphenylglyoxylate. DpgC performed a net four-electron oxidation of the benzylic carbon of DPA-CoA and the hydrolysis of the thioester bond to generate free CoA (PubMed:18004875, PubMed:17507985). DpgC has the ability to process a diverse range of substituted phenylacetyl-CoA substrates (PubMed:18004875).<ref>PMID:17507985</ref> <ref>PMID:18004875</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/np/2np9_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=2np9 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Dioxygenase 3D structures|Dioxygenase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | [[ | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| - | == | + | |
| - | < | + | |
[[Category: Streptomyces toyocaensis]] | [[Category: Streptomyces toyocaensis]] | ||
| - | [[Category: Bruner | + | [[Category: Bruner SD]] |
| - | [[Category: Fielding | + | [[Category: Fielding EN]] |
| - | [[Category: Widboom | + | [[Category: Widboom PF]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of a dioxygenase in the Crotonase superfamily
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