6G5R
Structure of the UB2H domain of E.coli PBP1B in complex with LpoB
Summary for 6G5R
| Entry DOI | 10.2210/pdb6g5r/pdb |
| Related | 2MII 3FWL 3VMA 4Q6Z 5FGZ 5HL9 6FZK |
| NMR Information | BMRB: 34255 |
| Descriptor | Penicillin-binding protein 1B (1 entity in total) |
| Functional Keywords | murein polymerase, complex, lpob, pbp1b, e. coli, transpeptidase, glycosyltransferase, peptidoglican, transferase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 1 |
| Total formula weight | 13183.97 |
| Authors | Simorre, J.P.,Maya Martinez, R.C.,Bougault, C. (deposition date: 2018-03-29, release date: 2019-02-20, Last modification date: 2024-06-19) |
| Primary citation | Egan, A.J.F.,Maya-Martinez, R.,Ayala, I.,Bougault, C.M.,Banzhaf, M.,Breukink, E.,Vollmer, W.,Simorre, J.P. Induced conformational changes activate the peptidoglycan synthase PBP1B. Mol. Microbiol., 110:335-356, 2018 Cited by PubMed Abstract: 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 polymerising (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. PubMed: 30044025DOI: 10.1111/mmi.14082 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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