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| | <StructureSection load='4unm' size='340' side='right'caption='[[4unm]], [[Resolution|resolution]] 1.77Å' scene=''> | | <StructureSection load='4unm' size='340' side='right'caption='[[4unm]], [[Resolution|resolution]] 1.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4unm]] is a 2 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=4UNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UNM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4unm]] is a 2 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=4UNM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UNM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4unm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4unm OCA], [http://pdbe.org/4unm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4unm RCSB], [http://www.ebi.ac.uk/pdbsum/4unm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4unm 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=4unm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4unm OCA], [https://pdbe.org/4unm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4unm RCSB], [https://www.ebi.ac.uk/pdbsum/4unm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4unm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D6EWM0_STRLI D6EWM0_STRLI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces lividans krasil'nikov et al. 1965]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chaplin, A K]] | + | [[Category: Streptomyces lividans]] |
| - | [[Category: Hough, M A]] | + | [[Category: Chaplin AK]] |
| - | [[Category: Worrall, J A.R]] | + | [[Category: Hough MA]] |
| - | [[Category: Copper oxidase]] | + | [[Category: Worrall JAR]] |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
D6EWM0_STRLI
Publication Abstract from PubMed
Streptomyces lividans displays a distinct dependence on copper to fully initiate morphological development. Evidence has accumulated to implicate the participation of an extracytoplasmic cuproenzyme in morphogenesis. In the present study, we show that GlxA fulfils all criteria to be that cuproenzyme. GlxA is membrane associated and has an active site consisting of a mononuclear copper and a cross-linked Y-C cofactor. The domain organization of the tertiary structure defines GlxA as a new structural member of the mono-copper oxidase family, with copper co-ordination geometry similar to, but spectroscopically distinct from fungal galactose oxidase (Gox). EPR spectroscopy reveals that the oxidation of cupric GlxA generates a protein radical residing on the Y-C cross-link. A variety of canonical Gox substrates (including D-galactose) were tested but none were readily turned over by GlxA. A glxA null-mutant leads to loss of glycan accumulation at hyphal tips and consequently a drastically changed morphology both on solid substrates and in liquid-grown environments, a scenario similarly observed in the absence of the neighbouring glycan synthase CslA (cellulase synthase-like protein). In addition the glxA mutant has lost the stimulation of development by copper, supporting a model whereby the enzymatic action of GlxA on the glycan is required for development and morphology. From a biotechnology perspective, the open mycelium morphology observed with the glxA mutant in submerged culture has implications for use as an enzyme production host.
GlxA is a new structural member of the radical copper oxidase family and is required for glycan deposition at hyphal tips and morphogenesis of Streptomyces lividans.,Chaplin AK, Petrus ML, Mangiameli G, Hough MA, Svistunenko DA, Nicholls P, Claessen D, Vijgenboom E, Worrall JA Biochem J. 2015 Aug 1;469(3):433-44. doi: 10.1042/BJ20150190. Epub 2015 Jun 11. PMID:26205496[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chaplin AK, Petrus ML, Mangiameli G, Hough MA, Svistunenko DA, Nicholls P, Claessen D, Vijgenboom E, Worrall JA. GlxA is a new structural member of the radical copper oxidase family and is required for glycan deposition at hyphal tips and morphogenesis of Streptomyces lividans. Biochem J. 2015 Aug 1;469(3):433-44. doi: 10.1042/BJ20150190. Epub 2015 Jun 11. PMID:26205496 doi:http://dx.doi.org/10.1042/BJ20150190
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