2fct

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[[Image:2fct.gif|left|200px]]
 
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{{Structure
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==SyrB2 with Fe(II), chloride, and alpha-ketoglutarate==
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|PDB= 2fct |SIZE=350|CAPTION= <scene name='initialview01'>2fct</scene>, resolution 1.60&Aring;
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<StructureSection load='2fct' size='340' side='right'caption='[[2fct]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=AKG:2-OXYGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>
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<table><tr><td colspan='2'>[[2fct]] 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=2FCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FCT FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.6&#8491;</td></tr>
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|GENE= SyrB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=321 Pseudomonas syringae pv. syringae])
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<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=CL:CHLORIDE+ION'>CL</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>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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|DOMAIN=
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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=2fct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fct OCA], [https://pdbe.org/2fct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fct RCSB], [https://www.ebi.ac.uk/pdbsum/2fct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fct ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fct OCA], [http://www.ebi.ac.uk/pdbsum/2fct PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fct RCSB]</span>
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== Function ==
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}}
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[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>
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== Evolutionary Conservation ==
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'''SyrB2 with Fe(II), chloride, and alpha-ketoglutarate'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fc/2fct_consurf.spt"</scriptWhenChecked>
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Non-haem Fe(II)/alpha-ketoglutarate (alphaKG)-dependent enzymes harness the reducing power of alphaKG to catalyse oxidative reactions, usually the hydroxylation of unactivated carbons, and are involved in processes such as natural product biosynthesis, the mammalian hypoxic response, and DNA repair. These enzymes couple the decarboxylation of alphaKG with the formation of a high-energy ferryl-oxo intermediate that acts as a hydrogen-abstracting species. All previously structurally characterized mononuclear iron enzymes contain a 2-His, 1-carboxylate motif that coordinates the iron. The two histidines and one carboxylate, known as the 'facial triad', form one triangular side of an octahedral iron coordination geometry. A subclass of mononuclear iron enzymes has been shown to catalyse halogenation reactions, rather than the more typical hydroxylation reaction. SyrB2, a member of this subclass, is a non-haem Fe(II)/alphaKG-dependent halogenase that catalyses the chlorination of threonine in syringomycin E biosynthesis. Here we report the structure of SyrB2 with both a chloride ion and alphaKG coordinated to the iron ion at 1.6 A resolution. This structure reveals a previously unknown coordination of iron, in which the carboxylate ligand of the facial triad is replaced by a chloride ion.
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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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==About this Structure==
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</jmolCheckbox>
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2FCT is a [[Single protein]] structure of sequence from [http://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=2FCT OCA].
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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=2fct ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis., Blasiak LC, Vaillancourt FH, Walsh CT, Drennan CL, Nature. 2006 Mar 16;440(7082):368-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16541079 16541079]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas syringae pv. syringae]]
[[Category: Pseudomonas syringae pv. syringae]]
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[[Category: Single protein]]
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[[Category: Blasiak LC]]
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[[Category: Blasiak, L C.]]
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[[Category: Drennan CL]]
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[[Category: Drennan, C L.]]
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[[Category: cupin]]
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[[Category: halogenase]]
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[[Category: mononuclear iron]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:00:59 2008''
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Current revision

SyrB2 with Fe(II), chloride, and alpha-ketoglutarate

PDB ID 2fct

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