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Crystal structures of two novel dye‐decolorizing peroxidases reveal a β‐barrel fold with a conserved heme‐binding motif
Author(s) -
Zubieta Chloe,
Krishna S. Sri,
Kapoor Mili,
Kozbial Piotr,
McMullan Daniel,
Axelrod Herbert L.,
Miller Mitchell D.,
Abdubek Polat,
Ambing Eileen,
Astakhova Tamara,
Carlton Dennis,
Chiu HsiuJu,
Clayton Thomas,
Deller Marc C.,
Duan Lian,
Elsliger MarcAndré,
Feuerhelm Julie,
Grzechnik Slawomir K.,
Hale Joanna,
Hampton Eric,
Han Gye Won,
Jaroszewski Lukasz,
Jin Kevin K.,
Klock Heath E.,
Knuth Mark W.,
Kumar Abhinav,
Marciano David,
Morse Andrew T.,
Nigoghossian Edward,
Okach Linda,
Oommachen Silvya,
Reyes Ron,
Rife Christopher L.,
Schimmel Paul,
Bedem Henry van den,
Weekes Dana,
White Aprilfawn,
Xu Qingping,
Hodgson Keith O.,
Wooley John,
Deacon Ashley M.,
Godzik Adam,
Lesley Scott A.,
Wilson Ian A.
Publication year - 2007
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21550
Subject(s) - heme , isothermal titration calorimetry , shewanella oneidensis , histidine , biochemistry , chemistry , binding site , stereochemistry , biology , bacteria , amino acid , enzyme , genetics
Bt DyP from Bacteroides thetaiotaomicron (strain VPI‐5482) and TyrA from Shewanella oneidensis are dye‐decolorizing peroxidases (DyPs), members of a new family of heme‐dependent peroxidases recently identified in fungi and bacteria. Here, we report the crystal structures of BtDyP and TyrA at 1.6 and 2.7 Å, respectively. BtDyP assembles into a hexamer, while TyrA assembles into a dimer; the dimerization interface is conserved between the two proteins. Each monomer exhibits a two‐domain, α+β ferredoxin‐like fold. A site for heme binding was identified computationally, and modeling of a heme into the proposed active site allowed for identification of residues likely to be functionally important. Structural and sequence comparisons with other DyPs demonstrate a conservation of putative heme‐binding residues, including an absolutely conserved histidine. Isothermal titration calorimetry experiments confirm heme binding, but with a stoichiometry of 0.3:1 (heme:protein). Proteins 2007. © 2007 Wiley‐Liss, Inc.