5dbj

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==Crystal structure of halogenase PltA==
==Crystal structure of halogenase PltA==
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<StructureSection load='5dbj' size='340' side='right' caption='[[5dbj]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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<StructureSection load='5dbj' size='340' side='right'caption='[[5dbj]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dbj]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DBJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dbj]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_protegens_Pf-5 Pseudomonas protegens Pf-5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DBJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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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]] 2.75&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkylhalidase Alkylhalidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.1 3.8.1.1] </span></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dbj OCA], [http://pdbe.org/5dbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dbj RCSB], [http://www.ebi.ac.uk/pdbsum/5dbj PDBsum]</span></td></tr>
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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=5dbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dbj OCA], [https://pdbe.org/5dbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dbj RCSB], [https://www.ebi.ac.uk/pdbsum/5dbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dbj ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLTA_PSEF5 PLTA_PSEF5] Involved in the biosynthesis of the antibiotic pyoluteorin (PubMed:16162666). Catalyzes the dichlorination of the pyrrole ring of pyrrolyl-S-PltL, generating the 5-chloropyrrolyl-S-PltL intermediate and then the 4,5-dichloropyrrolyl-S-PltL product (PubMed:16162666).<ref>PMID:16162666</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pyoluteorin is an antifungal agent composed of a 4,5-dichlorinated pyrrole group linked to a resorcinol moiety. The pyoluteorin biosynthetic gene cluster in Pseudomonas fluorescens Pf-5 encodes the halogenase PltA, which has been previously demonstrated to perform both chlorinations in vitro. PltA selectively accepts as a substrate a pyrrole moiety covalently tethered to a nonribosomal peptide thiolation domain PltL (pyrrolyl-S-PltL) for FAD-dependent di-chlorination, yielding 4,5-dichloropyrrolyl-S-PltL. We report a 2.75A-resolution crystal structure of PltA in complex with FAD and chloride. PltA is a dimeric enzyme, containing a flavin-binding fold conserved in flavin-dependent halogenases and monooxygenases, and an additional unique helical region at the C-terminus. This C-terminal region blocks a putative substrate-binding cleft, suggesting that a conformational change involving repositioning of this region is necessary to allow binding of the pyrrolyl-S-PltL substrate for its dichlorination by PltA.
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Crystal structure of halogenase PltA from the pyoluteorin biosynthetic pathway.,Pang AH, Garneau-Tsodikova S, Tsodikov OV J Struct Biol. 2015 Sep 28. pii: S1047-8477(15)30068-X. doi:, 10.1016/j.jsb.2015.09.013. PMID:26416533<ref>PMID:26416533</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5dbj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alkylhalidase]]
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[[Category: Large Structures]]
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[[Category: Pang, A H]]
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[[Category: Pseudomonas protegens Pf-5]]
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[[Category: Tsodikov, O V]]
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[[Category: Pang AH]]
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[[Category: Fad]]
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[[Category: Tsodikov OV]]
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[[Category: Flavoprotein]]
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[[Category: Halogenase]]
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[[Category: Pyoluteorin]]
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[[Category: Rossmann fold]]
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Crystal structure of halogenase PltA

PDB ID 5dbj

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