3NCX

Crystal structure of EHEC O157:H7 intimin mutant

Summary for 3NCX

• Entry DOI: 10.2210/pdb3ncx/pdb
• Related: 1F00 1F02 3NCW
• Descriptor: Intimin adherence protein (2 entities in total)
• Functional Keywords: intimin tir, cell adhesion
• Biological source: Escherichia coli O157:H7
• Total number of polymer chains: 2
• Total formula weight: 41444.34

Authors

Yi, Y.,Gao, F.,Gao, G.F.,Zou, Q.M. (deposition date: 2010-06-06, release date: 2011-01-05, Last modification date: 2024-10-16)

Primary citation

Yi, Y.,Ma, Y.,Gao, F.,Mao, X.,Peng, H.,Feng, Y.,Fan, Z.,Wang, G.,Guo, G.,Yan, J.,Zeng, H.,Zou, Q.M.,Gao, G.F.
Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC
Plos One, 5:e15285-e15285, 2010

PubMed Abstract: Enterohaemorrhagic E. coli (EHEC) O157:H7 is a primary food-borne bacterial pathogen capable of causing life-threatening human infections which poses a serious challenge to public health worldwide. Intimin, the bacterial outer-membrane protein, plays a key role in the initiating process of EHEC infection. This activity is dependent upon translocation of the intimin receptor (Tir), the intimin binding partner of the bacteria-encoded host cell surface protein. Intimin has attracted considerable attention due to its potential function as an antibacterial drug target. Here, we report the crystal structure of the Tir-binding domain of intimin (Int188) from E. coli O157:H7 at 2.8 Å resolution, together with a mutant (IntN916Y) at 2.6 Å. We also built the structural model of EHEC intimin-Tir complex and analyzed the key binding residues. It suggested that the binding pattern of intimin and Tir between EHEC and Enteropathogenic E. coli (EPEC) adopt a similar mode and they can complement with each other. Detailed structural comparison indicates that there are four major points of structural variations between EHEC and EPEC intimins: one in Domain I (Ig-like domain), the other three located in Domain II (C-type lectin-like domain). These variations result in different binding affinities. These findings provide structural insight into the binding pattern of intimin to Tir and the molecular mechanism of EHEC O157: H7.

PubMed: 21179574
DOI: 10.1371/journal.pone.0015285

Experimental method

X-RAY DIFFRACTION (2.6 Å)