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| | ==The Crystal Structure of a putative PTS IIB(PtxB) from Streptococcus mutans== | | ==The Crystal Structure of a putative PTS IIB(PtxB) from Streptococcus mutans== |
| - | <StructureSection load='3czc' size='340' side='right' caption='[[3czc]], [[Resolution|resolution]] 2.02Å' scene=''> | + | <StructureSection load='3czc' size='340' side='right'caption='[[3czc]], [[Resolution|resolution]] 2.02Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3czc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25175 Atcc 25175]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CZC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3czc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CZC FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.02Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ptxB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1309 ATCC 25175])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] </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=3czc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3czc OCA], [https://pdbe.org/3czc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3czc RCSB], [https://www.ebi.ac.uk/pdbsum/3czc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3czc ProSAT]</span></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=3czc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3czc OCA], [http://pdbe.org/3czc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3czc RCSB], [http://www.ebi.ac.uk/pdbsum/3czc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3czc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q93DB0_STRMG Q93DB0_STRMG] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/3czc_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cz/3czc_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 25175]] | + | [[Category: Large Structures]] |
| - | [[Category: Lei, J]] | + | [[Category: Streptococcus mutans]] |
| - | [[Category: Su, X D]] | + | [[Category: Lei J]] |
| - | [[Category: Alpha/beta sandwich]] | + | [[Category: Su XD]] |
| - | [[Category: Phosphotransferase system]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
Q93DB0_STRMG
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
Streptococcus mutans is the primary etiological agent of dental caries in man and other mammalian organisms. This bacterium metabolizes carbohydrates actively and thrives under anaerobic conditions by fermenting l-ascorbate (Asc) via the sga operon, which includes SgaT, PtxB, and PtxA. These three proteins are members of the Asc family of enzyme II (EII) complexes of the bacterial phosphotransferase system. Here, we report the crystal structure of PtxB, solved by single-wavelength anomalous dispersion phasing, and that of PtxA, solved by molecular replacement, from S. mutans. PtxB provides the first crystal structure of an EIIB from the Asc family, composed of a central beta sheet of parallel strands flanked by alpha helices on both sides. The structure of PtxB is similar to the structures of IIB(Mtl) (IIB subunit of mannitol PTS) and IIB(Cel) (IIB subunit of cellobiose) in Escherichia coli despite the low sequence identity. PtxA adopts a globular alpha/beta sandwich structure. The phosphorylation-site His68 is situated between beta2 and beta3, within a hydrophobic pocket. We found that the hydrogen bond on N(delta1) of the active-site histidine is a common means of ensuring that phosphate is on the correct N(varepsilon2) site in many EIIA families. Finally, a model of the PtxB-PtxA complex was constructed, and a PtxA-phospho-PtxB state is proposed. Analyses of the two structures shed light on the catalytic mechanism of the phosphotransferase system.
Crystal structures of phosphotransferase system enzymes PtxB (IIB(Asc)) and PtxA (IIA(Asc)) from Streptococcus mutans.,Lei J, Li LF, Su XD J Mol Biol. 2009 Feb 20;386(2):465-75. Epub 2008 Dec 25. PMID:19135450[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lei J, Li LF, Su XD. Crystal structures of phosphotransferase system enzymes PtxB (IIB(Asc)) and PtxA (IIA(Asc)) from Streptococcus mutans. J Mol Biol. 2009 Feb 20;386(2):465-75. Epub 2008 Dec 25. PMID:19135450 doi:10.1016/j.jmb.2008.12.046
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