View source for 5zw0


==Apo-form PigA==
<StructureSection load='5zw0' size='340' side='right'caption='[[5zw0]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zw0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_sp._ATCC_39006 Serratia sp. ATCC 39006]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZW0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54&#8491;</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=5zw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zw0 OCA], [https://pdbe.org/5zw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zw0 RCSB], [https://www.ebi.ac.uk/pdbsum/5zw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zw0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PIGA_SERS3 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].<ref>PMID:15853884</ref> <ref>PMID:17002325</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prodigiosin 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<ref>PMID:30095206</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zw0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Serratia sp. ATCC 39006]]
[[Category: Ko T-P]]
[[Category: Lee C-C]]
[[Category: Wang AHJ]]