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==Crystal structure of PigE: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp. FS14==
<StructureSection load='4ppm' size='340' side='right'caption='[[4ppm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ppm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_sp._FS14 Serratia sp. FS14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPM 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=4ppm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppm OCA], [https://pdbe.org/4ppm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppm RCSB], [https://www.ebi.ac.uk/pdbsum/4ppm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PIGE_SERSF PIGE_SERSF] Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the transamination to the aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which spontaneously cyclizes to yield the dihydro form of MAP (H2MAP).<ref>PMID:24704447</ref> 
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== Publication Abstract from PubMed ==
Prodigiosin, a tripyrrole red pigment synthesized by Serratia and some other microbes through a bifurcated biosynthesis pathway, MBC (4-methoxy-2,2'-bipyrrole-5-carbaldehyde) and MAP (2-methyl-3-n-amyl-pyrrole) are synthesized separately and then condensed by PigC to form prodigiosin. MAP is synthesized sequentially by PigD, PigE and PigB. PigE catalyzes the transamination of an amino group to the aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which spontaneously cyclizes to form H2MAP. Here we report the crystal structure of the catalytic domain of PigE which involved in the biosynthesis of prodigiosin precursor MAP for the first time to a resolution of 2.3A with a homodimer in the asymmetric unit. The monomer of PigE catalytic domain is composed of three domains with PLP as cofactor: a small N-terminal domain connecting the catalytic domain with the front part of PigE, a large PLP-binding domain and a C-terminal domain. The residues from both monomers build the PLP binding site at the interface of the dimer which resembles the other PLP-dependent enzymes. Structural comparison of PigE with Thermus thermophilus AcOAT showed a higher hydrophobic and smaller active site of PigE, these differences may be the reason for substrate specificity.

Crystal structure of the catalytic domain of PigE: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp. FS14.,Lou X, Ran T, Han N, Gao Y, He J, Tang L, Xu D, Wang W Biochem Biophys Res Commun. 2014 Apr 25;447(1):178-83. doi:, 10.1016/j.bbrc.2014.03.125. Epub 2014 Apr 2. PMID:24704447<ref>PMID:24704447</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4ppm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Serratia sp. FS14]]
[[Category: Lou XD]]
[[Category: Ran TT]]
[[Category: Wang WW]]
[[Category: Xu DQ]]