2fcv: Difference between revisions

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<StructureSection load='2fcv' size='340' side='right'caption='[[2fcv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2fcv' size='340' side='right'caption='[[2fcv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fcv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FCV FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fcv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FCV FirstGlance]. <br>
</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=BR:BROMIDE+ION'>BR</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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fct|2fct]], [[2fcu|2fcu]]</div></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=BR:BROMIDE+ION'>BR</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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SyrB2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=317 ATCC 19310])</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=2fcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fcv OCA], [https://pdbe.org/2fcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fcv RCSB], [https://www.ebi.ac.uk/pdbsum/2fcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fcv ProSAT]</span></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=2fcv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fcv OCA], [https://pdbe.org/2fcv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fcv RCSB], [https://www.ebi.ac.uk/pdbsum/2fcv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fcv ProSAT]</span></td></tr>
</table>
</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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2fcv ConSurf].
</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=2fcv ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:16541079<ref>PMID:16541079</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fcv" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 19310]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Blasiak, L C]]
[[Category: Pseudomonas syringae]]
[[Category: Drennan, C L]]
[[Category: Blasiak LC]]
[[Category: Biosynthetic protein]]
[[Category: Drennan CL]]
[[Category: Cupin]]
[[Category: Halogenase]]
[[Category: Mononuclear iron]]
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