View source for 2fcu


==SyrB2 with alpha-ketoglutarate==
<StructureSection load='2fcu' size='340' side='right'caption='[[2fcu]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fcu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._syringae Pseudomonas syringae pv. syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FCU 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=DSU:((2R,3S,4S,5S)-3,4-DIHYDROXY-5-(HYDROXYMETHYL)-5-((2R,3S,4S,5S,6R)-3,4,5-TRIHYDROXY-6-METHOXY-TETRAHYDRO-2H-PYRAN-2-YLOXY)-TETRAHYDROFURAN-2-YL)METHYL+NONANOATE'>DSU</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=2fcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fcu OCA], [https://pdbe.org/2fcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fcu RCSB], [https://www.ebi.ac.uk/pdbsum/2fcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fcu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYRB2_PSESY SYRB2_PSESY] Involved in the biosynthesis of syringomycin E, a cyclic lipodepsinonapeptide toxin with phytotoxic activity (PubMed:16002467, PubMed:16528784, PubMed:19245217). Catalyzes the chlorination of L-Thr to 4-Cl-L-Thr when the amino acid is tethered via a thioester linkage to a covalently bound phosphopantetheine cofactor of the carrier protein SyrB1 (L-Thr-S-SyrB1), in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate (PubMed:16002467, PubMed:16528784, PubMed:19245217). In vitro, can catalyze tandem chlorinations at the gamma-position of the threonyl-S-protein substrate (PubMed:16528784). Can also brominate L-Thr-S-SyrB1 in reactions performed with excess sodium bromide, but a preference for chloride versus bromide by a factor of 180 can be estimated by comparing the peak intensities (PubMed:16528784). In addition, in the presence of the nitrogenous anions NO2(-) or N3(-), SyrB2 can direct aliphatic nitration and azidation reactions by the same mechanism as the native halogenation reaction (PubMed:24463698).<ref>PMID:16002467</ref> <ref>PMID:16528784</ref> <ref>PMID:19245217</ref> <ref>PMID:24463698</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/fc/2fcu_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=2fcu ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas syringae pv. syringae]]
[[Category: Blasiak LC]]
[[Category: Drennan CL]]