5zw0: Difference between revisions

Revision as of 21:24, 28 October 2020

Apo-form PigA

Structural highlights

5zw0 is a 2 chain structure with sequence from Sers3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	pigA (SERS3)
Activity:	[peptidyl-carrier_protein_dehydrogenase L-prolyl-[peptidyl-carrier protein] dehydrogenase], with EC number 1.3.8.14
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Williamson NR, Simonsen HT, Ahmed RA, Goldet G, Slater H, Woodley L, Leeper FJ, Salmond GP. Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. Mol Microbiol. 2005 May;56(4):971-89. PMID:15853884 doi:https://dx.doi.org/10.1111/j.1365-2958.2005.04602.x
↑ Garneau-Tsodikova S, Dorrestein PC, Kelleher NL, Walsh CT. Protein assembly line components in prodigiosin biosynthesis: characterization of PigA,G,H,I,J. J Am Chem Soc. 2006 Oct 4;128(39):12600-1. PMID:17002325 doi:https://dx.doi.org/10.1021/ja063611l
↑ Lee CC, Ko TP, Chen CT, Chan YT, Lo SY, Chang JY, Chen YW, Chung TF, Hsieh HJ, Hsiao CD, Wang AH. Crystal structure of PigA, a prolyl thioester-oxidizing enzyme in prodigiosin biosynthesis. Chembiochem. 2018 Aug 10. doi: 10.1002/cbic.201800409. PMID:30095206 doi:https://dx.doi.org/10.1002/cbic.201800409

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Williamson NR, Simonsen HT, Ahmed RA, Goldet G, Slater H, Woodley L, Leeper FJ, Salmond GP. Biosynthesis of the red antibiotic, prodigiosin, in Serratia: identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway, definition of the terminal condensing enzyme, and implications for undecylprodigiosin biosynthesis in Streptomyces. Mol Microbiol. 2005 May;56(4):971-89. PMID:15853884 doi:https://dx.doi.org/10.1111/j.1365-2958.2005.04602.x

[2] Garneau-Tsodikova S, Dorrestein PC, Kelleher NL, Walsh CT. Protein assembly line components in prodigiosin biosynthesis: characterization of PigA,G,H,I,J. J Am Chem Soc. 2006 Oct 4;128(39):12600-1. PMID:17002325 doi:https://dx.doi.org/10.1021/ja063611l

[3] Lee CC, Ko TP, Chen CT, Chan YT, Lo SY, Chang JY, Chen YW, Chung TF, Hsieh HJ, Hsiao CD, Wang AH. Crystal structure of PigA, a prolyl thioester-oxidizing enzyme in prodigiosin biosynthesis. Chembiochem. 2018 Aug 10. doi: 10.1002/cbic.201800409. PMID:30095206 doi:https://dx.doi.org/10.1002/cbic.201800409

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[2]

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@@ Line 1: / Line 1: @@
 ==Apo-form PigA==
-<StructureSection load='5zw0' size='340' side='right' caption='[[5zw0]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
+<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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZW0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5zw0]] is a 2 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=5ZW0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZW0 FirstGlance]. <br>
-</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>
+</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='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=5zw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zw0 OCA], [http://pdbe.org/5zw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zw0 RCSB], [http://www.ebi.ac.uk/pdbsum/5zw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zw0 ProSAT]</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://proteopedia.org/fgij/fg.htm?mol=5zw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zw0 OCA], [http://pdbe.org/5zw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zw0 RCSB], [http://www.ebi.ac.uk/pdbsum/5zw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zw0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
+[[Category: Sers3]]
 [[Category: Ko, T P]]
 [[Category: Lee, C C]]

5zw0: Difference between revisions

Revision as of 21:24, 28 October 2020

Apo-form PigA

Structural highlights

Function

Publication Abstract from PubMed

References

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