6FZK
NMR structure of UB2H, regulatory domain of PBP1b from E. coli
Summary for 6FZK
| Entry DOI | 10.2210/pdb6fzk/pdb |
| Related | 3FWL 5HLA 5HLB 5HLD |
| NMR Information | BMRB: 34246 |
| Descriptor | Penicillin-binding protein 1B (1 entity in total) |
| Functional Keywords | ub2h domain of pbp1b, regulatory domain, transferase |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 1 |
| Total formula weight | 13183.97 |
| Authors | Simorre, J.P.,Maya Martinez, R.C.,Bougault, C.,Egan, A.J.F.,Vollmer, W. (deposition date: 2018-03-15, 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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