Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA.

Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Research Abstract Details 

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Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Abstract Text:

Chloe Zubieta,Rosanne Joseph,S Sri Krishna,Daniel McMullan,Mili Kapoor,Herbert L Axelrod,Mitchell D Miller,Polat Abdubek,Claire Acosta,Tamara Astakhova,Dennis Carlton,Hsiu-Ju Chiu,Thomas Clayton,Marc C Deller,Lian Duan,Ylva Elias, Elsliger,Julie Feuerhelm,Slawomir K Grzechnik,Joanna Hale,Gye Won Han,Lukasz Jaroszewski,Kevin K Jin,Heath E Klock,Mark W Knuth,Piotr Kozbial,Abhinav Kumar,David Marciano,Andrew T Morse,Kevin D Murphy,Edward Nigoghossian,Linda Okach,Silvya Oommachen,Ron Reyes,Christopher L Rife,Paul Schimmel,Christina V Trout,Henry van den Bedem,Dana Weekes,Aprilfawn White,Qingping Xu,Keith O Hodgson,John Wooley,Ashley M Deacon,Adam Godzik,Scott A Lesley,Ian A Wilson,

TyrA is a member of the dye-decolorizing peroxidase (DyP) family, a new family of heme-dependent peroxidase recently identified in fungi and bacteria. Here, we report the crystal structure of TyrA in complex with iron protoporphyrin (IX) at 2.3 A. TyrA is a dimer, with each monomer exhibiting a two-domain, alpha/beta ferredoxin-like fold. Both domains contribute to the heme-binding site. Co-crystallization in the presence of an excess of iron protoporphyrin (IX) chloride allowed for the unambiguous location of the active site and the specific residues involved in heme binding. The structure reveals a Fe-His-Asp triad essential for heme positioning, as well as a novel conformation of one of the heme propionate moieties compared to plant peroxidases. Structural comparison to the canonical DyP family member, DyP from Thanatephorus cucumeris (Dec 1), demonstrates conservation of this novel heme conformation, as well as residues important for heme binding. Structural comparisons with representative members from all classes of the plant, bacterial, and fungal peroxidase superfamily demonstrate that TyrA, and by extension the DyP family, adopts a fold different from all other structurally characterized heme peroxidases. We propose that a new superfamily be added to the peroxidase classification scheme to encompass the DyP family of heme peroxidases.

Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Publishing Authors By Initials

C Zubieta,R Joseph,SS Krishna,D McMullan,M Kapoor,HL Axelrod,MD Miller,P Abdubek,C Acosta,T Astakhova,D Carlton,HJ Chiu,T Clayton,MC Deller,L Duan,Y Elias,MA Elsliger,J Feuerhelm,SK Grzechnik,J Hale,GW Han,L Jaroszewski,KK Jin,HE Klock,MW Knuth,P Kozbial,A Kumar,D Marciano,AT Morse,KD Murphy,E Nigoghossian,L Okach,S Oommachen,R Reyes,CL Rife,P Schimmel,CV Trout,H van den Bedem,D Weekes,A White,Q Xu,KO Hodgson,J Wooley,AM Deacon,A Godzik,SA Lesley,IA Wilson,

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Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Proteins

VOLUME: 69

Page Numbers: 234-43

Journal Abbreviation: Proteins

ISSN: 1097-0134

DAY: 1

MONTH: Nov

YEAR: 2007

Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA. Information

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LANGUAGE: eng

NlmUniqueID: 8700181

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Grant and Affiliation Information for Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA.

AFFILIATION: Stanford Synchrotron Radiation Laboratory, Stanford University, Menlo Park, California, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: U54 GM074898

ACRONYM: GM

MEDLINETA: Proteins

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