5C22

Crystal structure of Zn-bound HlyD from E. coli

Summary for 5C22

• Entry DOI: 10.2210/pdb5c22/pdb
• Related: 5C21
• Descriptor: Chromosomal hemolysin D, ZINC ION (3 entities in total)
• Functional Keywords: hlyd, type i secretion system, zn sad, multicrystal averaging, protein transport
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 129234.21

Authors

Ha, N.C.,Kim, J.S. (deposition date: 2015-06-15, release date: 2016-02-17, Last modification date: 2024-03-20)

Primary citation

Kim, J.S.,Song, S.,Lee, M.,Lee, S.,Lee, K.,Ha, N.C.
Crystal Structure of a Soluble Fragment of the Membrane Fusion Protein HlyD in a Type I Secretion System of Gram-Negative Bacteria
Structure, 24:477-485, 2016

PubMed Abstract: The protein toxin HlyA of Escherichia coli is exported without a periplasmic intermediate by the type I secretion system (T1SS). The T1SS is composed of an inner membrane ABC transporter HlyB, an outer-membrane channel protein TolC, and a membrane fusion protein HlyD. However, the assembly of the T1SS remains to be elucidated. In this study, we determine the crystal structure of a part of the C-terminal periplasmic domain of HlyD. The long α-helical domain consisting of three α helices and a lipoyl domain was identified in the crystal structure. Based on the HlyD structure, we modeled the hexameric assembly of HlyD with a long α-helical barrel, which formed a complex with TolC in an intermeshing cogwheel-to-cogwheel manner, as observed in tripartite RND-type drug efflux pumps. These observations provide a structural blueprint for understanding the type I secretion system in pathogenic Gram-negative bacteria.

PubMed: 26833388
DOI: 10.1016/j.str.2015.12.012

Experimental method

X-RAY DIFFRACTION (2.302 Å)