8V24
LapB cytoplasmic domain in complex with LpxC
Summary for 8V24
| Entry DOI | 10.2210/pdb8v24/pdb |
| EMDB information | 42897 |
| Descriptor | Lipopolysaccharide assembly protein B, UDP-3-O-acyl-N-acetylglucosamine deacetylase, ZINC ION, ... (5 entities in total) |
| Functional Keywords | adaptor, complex, deacetylase, lps, lpxc, lapb(ycim), protein binding |
| Biological source | Escherichia coli CFT073 More |
| Total number of polymer chains | 4 |
| Total formula weight | 159132.75 |
| Authors | |
| Primary citation | Shu, S.,Tsutsui, Y.,Nathawat, R.,Mi, W. Dual function of LapB (YciM) in regulating Escherichia coli lipopolysaccharide synthesis. Proc.Natl.Acad.Sci.USA, 121:e2321510121-e2321510121, 2024 Cited by PubMed Abstract: Levels of lipopolysaccharide (LPS), an essential glycolipid on the surface of most gram-negative bacteria, are tightly controlled-making LPS synthesis a promising target for developing new antibiotics. adaptor protein LapB (YciM) plays an important role in regulating LPS synthesis by promoting degradation of LpxC, a deacetylase that catalyzes the first committed step in LPS synthesis. Under conditions where LPS is abundant, LapB recruits LpxC to the AAA+ protease FtsH for degradation. LapB achieves this by simultaneously interacting with FtsH through its transmembrane helix and LpxC through its cytoplasmic domain. Here, we describe a cryo-EM structure of the complex formed between LpxC and the cytoplasmic domain of LapB (LapB). The structure reveals how LapB exploits both its tetratricopeptide repeat (TPR) motifs and rubredoxin domain to interact with LpxC. Through both in vitro and in vivo analysis, we show that mutations at the LapB/LpxC interface prevent LpxC degradation. Unexpectedly, binding to LapB also inhibits the enzymatic activity of LpxC through allosteric effects reminiscent of LpxC activation by MurA in Our findings argue that LapB regulates LPS synthesis in two steps: In the first step, LapB inhibits the activity of LpxC, and in the second step, it commits LpxC to degradation by FtsH. PubMed: 38635633DOI: 10.1073/pnas.2321510121 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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