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| | <StructureSection load='4b3l' size='340' side='right'caption='[[4b3l]], [[Resolution|resolution]] 2.51Å' scene=''> | | <StructureSection load='4b3l' size='340' side='right'caption='[[4b3l]], [[Resolution|resolution]] 2.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b3l]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B3L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b3l]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B3L FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b3k|4b3k]]</div></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]] 2.51Å</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=4b3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3l OCA], [https://pdbe.org/4b3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b3l RCSB], [https://www.ebi.ac.uk/pdbsum/4b3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b3l 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=4b3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b3l OCA], [https://pdbe.org/4b3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b3l RCSB], [https://www.ebi.ac.uk/pdbsum/4b3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b3l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q99YP9_STRP1 Q99YP9_STRP1] |
| | <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: Micrococcus scarlatinae klein 1884]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brumer, H]] | + | [[Category: Streptococcus pyogenes]] |
| - | [[Category: Dabin, J]] | + | [[Category: Brumer H]] |
| - | [[Category: Davies, G J]] | + | [[Category: Dabin J]] |
| - | [[Category: Ekloef, J M]] | + | [[Category: Davies GJ]] |
| - | [[Category: Kongsaeree, P T]] | + | [[Category: Ekloef JM]] |
| - | [[Category: Stepper, J]] | + | [[Category: Kongsaeree PT]] |
| - | [[Category: Taylor, E J]] | + | [[Category: Stepper J]] |
| - | [[Category: Thongpoo, P]] | + | [[Category: Taylor EJ]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Thongpoo P]] |
| - | [[Category: Carbohydrate-active enzyme]]
| + | [[Category: Turkenburg JP]] |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q99YP9_STRP1
Publication Abstract from PubMed
The group A streptococcus Streptococcus pyogenes is the causative agent of a wide spectrum of invasive infections, including necrotizing fasciitis, scarlet fever and toxic shock syndrome. In the context of its carbohydrate chemistry, it is interesting that S. pyogenes (in this work strain M1 GAS SF370) displays a spectrum of oligosaccharide-processing enzymes that are located in close proximity on the genome but that the in vivo function of these proteins remains unknown. These proteins include different sugar transporters (SPy1593 and SPy1595), both GH125 alpha-1,6- and GH38 alpha-1,3-mannosidases (SPy1603 and SPy1604), a GH84 beta-hexosaminidase (SPy1600) and a putative GH2 beta-galactosidase (SPy1586), as well as SPy1599, a family GH1 `putative beta-glucosidase'. Here, the solution of the three-dimensional structure of SPy1599 in a number of crystal forms complicated by unusual crystallographic twinning is reported. The structure is a classical (beta/alpha)(8)-barrel, consistent with CAZy family GH1 and other members of the GH-A clan. SPy1599 has been annotated in sequence depositions as a beta-glucosidase (EC 3.2.1.21), but no such activity could be found; instead, three-dimensional structural overlaps with other enzymes of known function suggested that SPy1599 contains a phosphate-binding pocket in the active site and has possible 6-phospho-beta-glycosidase activity. Subsequent kinetic analysis indeed showed that SPy1599 has 6-phospho-beta-glucosidase (EC 3.2.1.86) activity. These data suggest that SPy1599 is involved in the intracellular degradation of 6-phosphoglycosides, which are likely to originate from import through one of the organism's many phosphoenolpyruvate phosphotransfer systems (PEP-PTSs).
Structure and activity of the Streptococcus pyogenes family GH1 6-phospho-beta-glucosidase SPy1599.,Stepper J, Dabin J, Eklof JM, Thongpoo P, Kongsaeree P, Taylor EJ, Turkenburg JP, Brumer H, Davies GJ Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):16-23. doi:, 10.1107/S0907444912041005. Epub 2012 Dec 20. PMID:23275159[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stepper J, Dabin J, Eklof JM, Thongpoo P, Kongsaeree P, Taylor EJ, Turkenburg JP, Brumer H, Davies GJ. Structure and activity of the Streptococcus pyogenes family GH1 6-phospho-beta-glucosidase SPy1599. Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):16-23. doi:, 10.1107/S0907444912041005. Epub 2012 Dec 20. PMID:23275159 doi:http://dx.doi.org/10.1107/S0907444912041005
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