MF7000973 PigE (Serratia sp. FS14) 4ppm X-ray 2.30 Homodimer Serratia sp 24704447 Lou X, Ran T, Han N, Gao Y, He J, Tang L, Xu D, Wang W Biochem. Biophys. Res. Commun. 2014 1 447 178-83 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 2.3Å 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. GO:0042802 identical protein binding GO:0070280 pyridoxal binding GO:0030170 pyridoxal phosphate binding GO:0008483 transaminase activity GO:0017000 antibiotic biosynthetic process 2 1 Homooligomeric enzymes Homodimeric enzymes All chains according to the most probable oligomerization state stored in PDBe were considered. A Aminotransferase PigE Serratia sp A0A0J9X1Q5 372 853 56% MKFGFIAHPTSLGLKRYVKMLDLLQRNSTEQHSGYTRELWERQNLVPFMNFARITSATGATCEGVIKYMPLVADEMLADARGIAARVVQGIEELAGDGAELVGLGGFTSIVGRRGEATAEKSPVPVTSGNSLTTYAGYKALMQIQSWLEIRPEEEPVAIVGYPGSICLALSRLLLAHGFSLHLLHRAGNHDRSELLSHLPEEYHSRVTLTSDPEDLYPRCKLFAAATSAGGVIDPARLQPGSIFIDVALPRDIASETRPARDDILIIDGGCVTATDAVKLGGESLNVTIKQQLNGCMAETIVLALENRRENFSLGRYLAPEKVLEIGEIAERHGFFAYPLASYGERIDRQSVTNLKRYYHHDIYAGESADAALPASRLAFIDAVIAQTPAREDTLDRYHQYINPMMVDFLKLQRCDNVFRSAAGTQLYDDAGEAFLDMVAGYGCLNLGHNPQPVVNALKNYLDAQGPNFIQYISIPEQTAKLAEVLCRLAPGNMGRVFFSNSGTEAVEAAMKIAKASTGKPGIAYLRNSYHGKTLGALSITGRDKHRRYFTPLLDAMVEVPFGDLAALREALNREDVGALMIEPIQGEGGVHIPPAGYLQAVQQLCRETGVLLMVDEVQTGLGRTGKLFACEWDGIEPDVLMLSKSLSGGLIPIGATLCRADLWQKAYGTADRFLVHSSTYGGGNLASVVALSALREILAQDLVGHAERMGAYFKQALSEIAARYPFVSEVRGRGLMLGIQFDQAFTGAVNASAREFATRLPGDWHTTWKFLPDPVQAHLRAAMDRMEQALGEMFCMKFVTKLCQDHKILTFITANSSTVIRIQPPLIISKAEIDRFVGAFATVCEELSTFLD 853 secondary structure helix 376 387 secondary structure helix 390 402 secondary structure helix 403 413 secondary structure helix 440 444 secondary structure helix 451 464 secondary structure helix 476 490 secondary structure helix 502 519 secondary structure helix 534 539 secondary structure helix 543 548 secondary structure helix 564 574 secondary structure helix 597 609 secondary structure helix 629 634 secondary structure helix 644 649 secondary structure helix 660 669 secondary structure helix 684 701 secondary structure helix 702 723 secondary structure helix 766 771 secondary structure helix 773 808 secondary structure helix 830 852 secondary structure strand 419 423 secondary structure strand 426 429 secondary structure strand 434 437 secondary structure strand 496 500 secondary structure strand 522 526 secondary structure strand 557 560 secondary structure strand 577 582 secondary structure strand 612 616 secondary structure strand 640 643 secondary structure strand 655 659 secondary structure strand 728 734 secondary structure strand 737 742 secondary structure strand 809 810 secondary structure strand 812 813 secondary structure strand 820 823 pfam PF00202 Aminotransferase class-III 420 843 B Aminotransferase PigE Serratia sp A0A0J9X1Q5 372 853 56% MKFGFIAHPTSLGLKRYVKMLDLLQRNSTEQHSGYTRELWERQNLVPFMNFARITSATGATCEGVIKYMPLVADEMLADARGIAARVVQGIEELAGDGAELVGLGGFTSIVGRRGEATAEKSPVPVTSGNSLTTYAGYKALMQIQSWLEIRPEEEPVAIVGYPGSICLALSRLLLAHGFSLHLLHRAGNHDRSELLSHLPEEYHSRVTLTSDPEDLYPRCKLFAAATSAGGVIDPARLQPGSIFIDVALPRDIASETRPARDDILIIDGGCVTATDAVKLGGESLNVTIKQQLNGCMAETIVLALENRRENFSLGRYLAPEKVLEIGEIAERHGFFAYPLASYGERIDRQSVTNLKRYYHHDIYAGESADAALPASRLAFIDAVIAQTPAREDTLDRYHQYINPMMVDFLKLQRCDNVFRSAAGTQLYDDAGEAFLDMVAGYGCLNLGHNPQPVVNALKNYLDAQGPNFIQYISIPEQTAKLAEVLCRLAPGNMGRVFFSNSGTEAVEAAMKIAKASTGKPGIAYLRNSYHGKTLGALSITGRDKHRRYFTPLLDAMVEVPFGDLAALREALNREDVGALMIEPIQGEGGVHIPPAGYLQAVQQLCRETGVLLMVDEVQTGLGRTGKLFACEWDGIEPDVLMLSKSLSGGLIPIGATLCRADLWQKAYGTADRFLVHSSTYGGGNLASVVALSALREILAQDLVGHAERMGAYFKQALSEIAARYPFVSEVRGRGLMLGIQFDQAFTGAVNASAREFATRLPGDWHTTWKFLPDPVQAHLRAAMDRMEQALGEMFCMKFVTKLCQDHKILTFITANSSTVIRIQPPLIISKAEIDRFVGAFATVCEELSTFLD 853 secondary structure helix 376 387 secondary structure helix 390 402 secondary structure helix 403 414 secondary structure helix 439 443 secondary structure helix 451 464 secondary structure helix 476 490 secondary structure helix 502 519 secondary structure helix 534 539 secondary structure helix 543 548 secondary structure helix 549 551 secondary structure helix 564 574 secondary structure helix 597 609 secondary structure helix 629 635 secondary structure helix 644 649 secondary structure helix 660 669 secondary structure helix 684 701 secondary structure helix 702 723 secondary structure helix 765 771 secondary structure helix 773 808 secondary structure helix 830 847 secondary structure helix 848 853 secondary structure strand 421 423 secondary structure strand 426 428 secondary structure strand 434 437 secondary structure strand 496 500 secondary structure strand 522 526 secondary structure strand 559 560 secondary structure strand 577 582 secondary structure strand 612 616 secondary structure strand 640 643 secondary structure strand 655 659 secondary structure strand 728 734 secondary structure strand 737 742 secondary structure strand 809 810 secondary structure strand 812 813 secondary structure strand 820 823 pfam PF00202 Aminotransferase class-III 420 843 Direct evidence The full structure participates in mutual synergistic folding. Aminotransferase class-III The equilibrium unfolding of pig liver 4-aminobutyrate aminotransferase by urea was found to be a cooperative process. The kinetic results indicated that the aminotransferase unfolds in a single kinetic phase (PMID:8075151). A N/A B N/A MF2110019 MF7000973