3e4y | pdb_00003e4y

Crystal structure of a 33kDa catalase-related protein from Mycobacterium avium subsp. paratuberculosis. I2(1)2(1)2(1) crystal form

spinqualitylabelsall models 3e4y, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3e4y is a 1 chain structure with sequence from Mycobacterium avium subsp. paratuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: GOL, HEM, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CRPE_MYCPA Has an organic peroxide-dependent peroxidase activity. Exhibits strong peroxidase activity using organic hydroperoxides as cosubstrates, weak peroxidase activity using hydrogen peroxide and negligible catalase activity. May have a role in elimination of reactive oxygen species, in particular by deactivating hydroperoxides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed True catalases are tyrosine-liganded, usually tetrameric, hemoproteins with subunit sizes of approximately 55-84 kDa. Recently characterized hemoproteins with a catalase-related structure, yet lacking in catalatic activity, include the 40-43 kDa allene oxide synthases of marine invertebrates and cyanobacteria. Herein, we describe the 1.8 A X-ray crystal structure of a 33 kDa subunit hemoprotein from Mycobacterium avium ssp. paratuberculosis (annotated as MAP-2744c), that retains the core elements of the catalase fold and exhibits an organic peroxide-dependent peroxidase activity. MAP-2744c exhibits negligible catalatic activity, weak peroxidatic activity using hydrogen peroxide (20/s) and strong peroxidase activity ( approximately 300/s) using organic hydroperoxides as co-substrate. Key amino acid differences significantly impact prosthetic group conformation and placement and confer a distinct activity to this prototypical member of a group of conserved bacterial "minicatalases". Its structural features and the result of the enzyme assays support a role for MAP-2744c and its close homologues in mitigating challenge by a variety of reactive oxygen species. The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis.,Pakhomova S, Gao B, Boeglin WE, Brash AR, Newcomer ME Protein Sci. 2009 Dec;18(12):2559-68. PMID:19827095 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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