YhdP forms an envelope-spanning phospholipid-binding bridge in complex with DedD

Cryo-EM shows purified endogenous YhdP forms an envelope-spanning, continuous-cavity structure that binds DedD, and its groove accommodates all major E. coli phospholipid classes without headgroup preference.

• Why it matters: How phospholipids synthesized at the inner membrane cross the periplasm is unresolved, and YhdP is a leading candidate for anterograde transfer.
• What they did: The authors purified YhdP at endogenous levels and used cryo-electron microscopy, proteomics, liposome co-sedimentation, single-molecule tracking, and native mass spectrometry to map structure and lipid binding.
• The result: YhdP’s C-terminal helices bind membranes directly, endogenous YhdP is as immobile as an outer membrane protein in vivo, and DedD engagement increases lipid density at the groove entrance, consistent with lipid loading.

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