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| | <StructureSection load='1a8q' size='340' side='right'caption='[[1a8q]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='1a8q' size='340' side='right'caption='[[1a8q]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1a8q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10762 Atcc 10762]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1A8Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1a8q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8Q FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BPOA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1894 ATCC 10762])</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]] 1.75Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </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=1a8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8q OCA], [https://pdbe.org/1a8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8q RCSB], [https://www.ebi.ac.uk/pdbsum/1a8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8q ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1a8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8q OCA], [http://pdbe.org/1a8q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a8q RCSB], [http://www.ebi.ac.uk/pdbsum/1a8q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BPA1_STRAU BPA1_STRAU]] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. | + | [https://www.uniprot.org/uniprot/CPOA1_KITAU CPOA1_KITAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. Able to brominate as well.<ref>PMID:1783900</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 10762]] | + | [[Category: Kitasatospora aureofaciens]] |
| - | [[Category: Chloride peroxidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Altenbuchner, J]] | + | [[Category: Altenbuchner J]] |
| - | [[Category: Hecht, H J]] | + | [[Category: Hecht H-J]] |
| - | [[Category: Hofmann, B]] | + | [[Category: Hofmann B]] |
| - | [[Category: Pee, K H.Van]]
| + | [[Category: Pelletier I]] |
| - | [[Category: Pelletier, I]] | + | [[Category: Toelzer S]] |
| - | [[Category: Toelzer, S]] | + | [[Category: Van Pee K-H]] |
| - | [[Category: Haloperoxidase]] | + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
CPOA1_KITAU May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. Able to brominate as well.[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
The structures of cofactor-free haloperoxidases from Streptomyces aureofaciens, Streptomyces lividans, and Pseudomonas fluorescens have been determined at resolutions between 1.9 A and 1.5 A. The structures of two enzymes complexed with benzoate or propionate identify the binding site for the organic acids which are required for the haloperoxidase activity. Based on these complexes and on the structure of an inactive variant, a reaction mechanism is proposed for the halogenation reaction with peroxoacid and hypohalous acid as reaction intermediates. Comparison of the structures suggests that a specific halide binding site is absent in the enzymes but that hydrophobic organic compounds may fit into the active site pocket for halogenation at preferential sites.
Structural investigation of the cofactor-free chloroperoxidases.,Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weng M, Pfeifer O, Krauss S, Lingens F, van Pée KH. Purification, characterization and comparison of two non-haem bromoperoxidases from Streptomyces aureofaciens ATCC 10762. J Gen Microbiol. 1991 Nov;137(11):2539-46. PMID:1783900 doi:10.1099/00221287-137-11-2539
- ↑ Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ. Structural investigation of the cofactor-free chloroperoxidases. J Mol Biol. 1998 Jun 19;279(4):889-900. PMID:9642069 doi:http://dx.doi.org/10.1006/jmbi.1998.1802
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