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| | <StructureSection load='3e4y' size='340' side='right'caption='[[3e4y]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='3e4y' size='340' side='right'caption='[[3e4y]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3e4y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_paratuberculosis"_(bergey_et_al._1923)_krasil'nikov_1941 "bacillus paratuberculosis" (bergey et al. 1923) krasil'nikov 1941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3e4y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_avium_subsp._paratuberculosis Mycobacterium avium subsp. paratuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e4w|3e4w]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAP_2744c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1770 "Bacillus paratuberculosis" (Bergey et al. 1923) Krasil'nikov 1941])</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=3e4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4y OCA], [https://pdbe.org/3e4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e4y RCSB], [https://www.ebi.ac.uk/pdbsum/3e4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4y ProSAT]</span></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=3e4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4y OCA], [https://pdbe.org/3e4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e4y RCSB], [https://www.ebi.ac.uk/pdbsum/3e4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CRPE_MYCPA 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.<ref>PMID:19827095</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Newcomer, M E]] | + | [[Category: Mycobacterium avium subsp. paratuberculosis]] |
| - | [[Category: Pakhomova, S]] | + | [[Category: Newcomer ME]] |
| - | [[Category: Catalase]] | + | [[Category: Pakhomova S]] |
| - | [[Category: Heme enzyme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| Structural highlights
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pakhomova S, Gao B, Boeglin WE, Brash AR, Newcomer ME. The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis. Protein Sci. 2009 Dec;18(12):2559-68. PMID:19827095 doi:10.1002/pro.265
- ↑ Pakhomova S, Gao B, Boeglin WE, Brash AR, Newcomer ME. The structure and peroxidase activity of a 33-kDa catalase-related protein from Mycobacterium avium ssp. paratuberculosis. Protein Sci. 2009 Dec;18(12):2559-68. PMID:19827095 doi:10.1002/pro.265
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