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| | ==Structure of the UB2H domain of E.coli PBP1B in complex with LpoB== | | ==Structure of the UB2H domain of E.coli PBP1B in complex with LpoB== |
| - | <StructureSection load='6g5r' size='340' side='right' caption='[[6g5r]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6g5r' size='340' side='right'caption='[[6g5r]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6g5r]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G5R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G5R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6g5r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G5R FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hl9|5hl9]], [[3fwl|3fwl]], [[3vma|3vma]], [[5fgz|5fgz]], [[2mii|2mii]], [[4q6z|4q6z]], [[6fzk|6fzk]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6g5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g5r OCA], [http://pdbe.org/6g5r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g5r RCSB], [http://www.ebi.ac.uk/pdbsum/6g5r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g5r 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=6g5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g5r OCA], [https://pdbe.org/6g5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g5r RCSB], [https://www.ebi.ac.uk/pdbsum/6g5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g5r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PBPB_ECOLI PBPB_ECOLI]] Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). | + | [https://www.uniprot.org/uniprot/PBPB_ECOLI PBPB_ECOLI] Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). |
| | <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 6g5r" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6g5r" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bougault, C]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Martinez, R C.Maya]]
| + | [[Category: Large Structures]] |
| - | [[Category: Simorre, J P]]
| + | [[Category: Bougault C]] |
| - | [[Category: Complex]]
| + | [[Category: Maya Martinez RC]] |
| - | [[Category: E. coli]]
| + | [[Category: Simorre JP]] |
| - | [[Category: Glycosyltransferase]] | + | |
| - | [[Category: Lpob]] | + | |
| - | [[Category: Murein polymerase]] | + | |
| - | [[Category: Pbp1b]] | + | |
| - | [[Category: Peptidoglican]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transpeptidase]]
| + | |
| Structural highlights
Function
PBPB_ECOLI Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Publication Abstract from PubMed
Bacteria surround their cytoplasmic membrane with an essential, stress-bearing peptidoglycan (PG) layer consisting of glycan chains linked by short peptides into a mesh-like structure. Growing and dividing cells expand their PG layer using inner-membrane anchored PG synthases, including Penicillin-binding proteins (PBPs), which participate in dynamic protein complexes to facilitate cell wall growth. In Escherichia coli, and presumably other Gram-negative bacteria, growth of the mainly single layered PG is regulated by outer membrane-anchored lipoproteins. The lipoprotein LpoB is required to activate PBP1B, which is a major, bi-functional PG synthase with glycan chain polymerizing (glycosyltransferase) and peptide cross-linking (transpeptidase) activities. In this work we show how the binding of LpoB to the regulatory UB2H domain of PBP1B activates both activities. Binding induces structural changes in the UB2H domain, which transduce to the two catalytic domains by distinct allosteric pathways. We also show how an additional regulator protein, CpoB, is able to selectively modulate the TPase activation by LpoB without interfering with GTase activation. This article is protected by copyright. All rights reserved.
Induced conformational changes activate the peptidoglycan synthase PBP1B.,Egan AJF, Maya-Martinez R, Ayala I, Bougault CM, Banzhaf M, Breukink E, Vollmer W, Simorre JP Mol Microbiol. 2018 Jul 25. doi: 10.1111/mmi.14082. PMID:30044025[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Egan AJF, Maya-Martinez R, Ayala I, Bougault CM, Banzhaf M, Breukink E, Vollmer W, Simorre JP. Induced conformational changes activate the peptidoglycan synthase PBP1B. Mol Microbiol. 2018 Jul 25. doi: 10.1111/mmi.14082. PMID:30044025 doi:http://dx.doi.org/10.1111/mmi.14082
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