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| | <StructureSection load='6pl5' size='340' side='right'caption='[[6pl5]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='6pl5' size='340' side='right'caption='[[6pl5]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6pl5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PL5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6pl5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PL5 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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]] 3.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rodA, TTHA1241 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8]), TTHA1191 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</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=6pl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pl5 OCA], [https://pdbe.org/6pl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pl5 RCSB], [https://www.ebi.ac.uk/pdbsum/6pl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pl5 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidoglycan_glycosyltransferase Peptidoglycan glycosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.129 2.4.1.129] </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=6pl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pl5 OCA], [http://pdbe.org/6pl5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pl5 RCSB], [http://www.ebi.ac.uk/pdbsum/6pl5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pl5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q5SIX3_THET8 Q5SIX3_THET8]] Peptidoglycan polymerase that is essential for cell wall elongation.[HAMAP-Rule:MF_02079] | + | [https://www.uniprot.org/uniprot/Q5SIX3_THET8 Q5SIX3_THET8] Peptidoglycan polymerase that is essential for cell wall elongation.[HAMAP-Rule:MF_02079] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6pl5" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6pl5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] |
| | + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidoglycan glycosyltransferase]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Thet8]]
| + | [[Category: Bernhardt TG]] |
| - | [[Category: Bernhardt, T G]] | + | [[Category: Erlandson SC]] |
| - | [[Category: Erlandson, S C]] | + | [[Category: Kruse AC]] |
| - | [[Category: Kruse, A C]] | + | [[Category: Rohs PDA]] |
| - | [[Category: Rohs, P D.A]] | + | [[Category: Rudner DZ]] |
| - | [[Category: Rudner, D Z]] | + | [[Category: Sjodt M]] |
| - | [[Category: Sjodt, M]] | + | [[Category: Zheng S]] |
| - | [[Category: Zheng, S]] | + | |
| - | [[Category: Elongasome]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Peptidoglycan transpeptidase]]
| + | |
| - | [[Category: Shape elongation division and sporulation]]
| + | |
| - | [[Category: Transmembrane protein]]
| + | |
| Structural highlights
Function
Q5SIX3_THET8 Peptidoglycan polymerase that is essential for cell wall elongation.[HAMAP-Rule:MF_02079]
Publication Abstract from PubMed
The shape, elongation, division and sporulation (SEDS) proteins are a highly conserved family of transmembrane glycosyltransferases that work in concert with class B penicillin-binding proteins (bPBPs) to build the bacterial peptidoglycan cell wall(1-6). How these proteins coordinate polymerization of new glycan strands with their crosslinking to the existing peptidoglycan meshwork is unclear. Here, we report the crystal structure of the prototypical SEDS protein RodA from Thermus thermophilus in complex with its cognate bPBP at 3.3 A resolution. The structure reveals a 1:1 stoichiometric complex with two extensive interaction interfaces between the proteins: one in the membrane plane and the other at the extracytoplasmic surface. When in complex with a bPBP, RodA shows an approximately 10 A shift of transmembrane helix 7 that exposes a large membrane-accessible cavity. Negative-stain electron microscopy reveals that the complex can adopt a variety of different conformations. These data define the bPBP pedestal domain as the key allosteric activator of RodA both in vitro and in vivo, explaining how a SEDS-bPBP complex can coordinate its dual enzymatic activities of peptidoglycan polymerization and crosslinking to build the cell wall.
Structural coordination of polymerization and crosslinking by a SEDS-bPBP peptidoglycan synthase complex.,Sjodt M, Rohs PDA, Gilman MSA, Erlandson SC, Zheng S, Green AG, Brock KP, Taguchi A, Kahne D, Walker S, Marks DS, Rudner DZ, Bernhardt TG, Kruse AC Nat Microbiol. 2020 Mar 9. pii: 10.1038/s41564-020-0687-z. doi:, 10.1038/s41564-020-0687-z. PMID:32152588[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sjodt M, Rohs PDA, Gilman MSA, Erlandson SC, Zheng S, Green AG, Brock KP, Taguchi A, Kahne D, Walker S, Marks DS, Rudner DZ, Bernhardt TG, Kruse AC. Structural coordination of polymerization and crosslinking by a SEDS-bPBP peptidoglycan synthase complex. Nat Microbiol. 2020 Mar 9. pii: 10.1038/s41564-020-0687-z. doi:, 10.1038/s41564-020-0687-z. PMID:32152588 doi:http://dx.doi.org/10.1038/s41564-020-0687-z
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