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| | <StructureSection load='1a88' size='340' side='right'caption='[[1a88]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1a88' size='340' side='right'caption='[[1a88]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1a88]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A88 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1A88 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1a88]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A88 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPO-L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 "Actinomyces lividans" Krasil'nikov et al. 1965])</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]] 1.9Å</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=1a88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a88 OCA], [https://pdbe.org/1a88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a88 RCSB], [https://www.ebi.ac.uk/pdbsum/1a88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a88 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=1a88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a88 OCA], [http://pdbe.org/1a88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a88 RCSB], [http://www.ebi.ac.uk/pdbsum/1a88 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a88 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PRXC_STRLI PRXC_STRLI] |
| | == 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: Actinomyces lividans krasil'nikov et al. 1965]] | |
| - | [[Category: Chloride peroxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Altenbuchner, J]] | + | [[Category: Streptomyces lividans]] |
| - | [[Category: Hecht, H J]] | + | [[Category: Altenbuchner J]] |
| - | [[Category: Hofmann, B]] | + | [[Category: Hecht H-J]] |
| - | [[Category: Pee, K H.Van]] | + | [[Category: Hofmann B]] |
| - | [[Category: Pelletier, I]] | + | [[Category: Pelletier I]] |
| - | [[Category: Toelzer, S]] | + | [[Category: Toelzer S]] |
| - | [[Category: Haloperoxidase]] | + | [[Category: Van Pee K-H]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
PRXC_STRLI
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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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