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| | ==Crystal structure of halogenase PltA== | | ==Crystal structure of halogenase PltA== |
| - | <StructureSection load='5dbj' size='340' side='right' caption='[[5dbj]], [[Resolution|resolution]] 2.75Å' scene=''> | + | <StructureSection load='5dbj' size='340' side='right'caption='[[5dbj]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <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> | + | <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> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
| - | <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> | + | <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> |
| - | <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> | + | <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> |
| | + | == Function == |
| | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alkylhalidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pang, A H]] | + | [[Category: Pseudomonas protegens Pf-5]] |
| - | [[Category: Tsodikov, O V]] | + | [[Category: Pang AH]] |
| - | [[Category: Fad]] | + | [[Category: Tsodikov OV]] |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Halogenase]]
| + | |
| - | [[Category: Pyoluteorin]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
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).[1]
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dorrestein PC, Yeh E, Garneau-Tsodikova S, Kelleher NL, Walsh CT. Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesis. Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):13843-8. PMID:16162666 doi:10.1073/pnas.0506964102
- ↑ Pang AH, Garneau-Tsodikova S, Tsodikov OV. Crystal structure of halogenase PltA from the pyoluteorin biosynthetic pathway. J Struct Biol. 2015 Sep 28. pii: S1047-8477(15)30068-X. doi:, 10.1016/j.jsb.2015.09.013. PMID:26416533 doi:http://dx.doi.org/10.1016/j.jsb.2015.09.013
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