5zw2: Difference between revisions
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==FAD complex of PigA== | ==FAD complex of PigA== | ||
<StructureSection load='5zw2' size='340' side='right' caption='[[5zw2]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5zw2' size='340' side='right'caption='[[5zw2]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5zw2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZW2 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5zw2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sers3 Sers3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZW2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZW2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=O4B:1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE'>O4B</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=O4B:1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE'>O4B</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zw0|5zw0]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zw0|5zw0]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pigA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=104623 SERS3])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-prolyl-[peptidyl-carrier_protein]_dehydrogenase L-prolyl-[peptidyl-carrier protein] dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.14 1.3.8.14] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-prolyl-[peptidyl-carrier_protein]_dehydrogenase L-prolyl-[peptidyl-carrier protein] dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.8.14 1.3.8.14] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zw2 OCA], [http://pdbe.org/5zw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zw2 RCSB], [http://www.ebi.ac.uk/pdbsum/5zw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zw2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Sers3]] | |||
[[Category: Ko, T P]] | [[Category: Ko, T P]] | ||
[[Category: Lee, C C]] | [[Category: Lee, C C]] | ||
Revision as of 00:24, 29 October 2020
FAD complex of PigAFAD complex of PigA
Structural highlights
Function[PIGA_SERS3] Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the desaturation of the L-prolyl-[PigG] to yield 1H-pyrrole-2-carbonyl-[PigG].[1] [2] Publication Abstract from PubMedProdigiosin is an intensely red pigment comprising three pyrroles. The biosynthetic pathway includes a two-step proline oxidation catalyzed by PigA, using FAD as its cofactor. Here the enzyme is crystallized in apo-form and in complex with FAD and proline. As an acyl-CoA dehydrogenase (ACAD) family member, the protein folds into a beta-sheet flanked by two alpha-helical domains. PigA forms a tetramer, consistent with analytical ultracentrifugation results. FAD binds to PigA in a similar way to that in the other ACAD-family enzymes. The variable conformations of loop beta4-beta5 and helix alphaG correlate well with the structural flexibility required for substrate entrance to the Re side of FAD. Modeling with PigG, the acyl carrier protein, suggests a reasonable mode of interaction with PigA. The structure helps explain the proline oxidation mechanism, in which Glu244 plays a central role by abstracting the substrate protons. It also reveals a plausible pocket for oxygen binding to the Si side of FAD. Crystal structure of PigA, a prolyl thioester-oxidizing enzyme in prodigiosin biosynthesis.,Lee CC, Ko TP, Chen CT, Chan YT, Lo SY, Chang JY, Chen YW, Chung TF, Hsieh HJ, Hsiao CD, Wang AH Chembiochem. 2018 Aug 10. doi: 10.1002/cbic.201800409. PMID:30095206[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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