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3B0Z

Crystal structure of cytoplasmic domain of FlhB from Salmonella typhimurium

Summary for 3B0Z
Entry DOI10.2210/pdb3b0z/pdb
Related3b1s
DescriptorFlagellar biosynthetic protein flhB, ZINC ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsflagella, type iii secretion system, protein transport, membrane protein
Biological sourceSalmonella enterica subsp. enterica serovar Typhimurium
More
Cellular locationCell inner membrane ; Multi- pass membrane protein : P40727 P40727
Total number of polymer chains2
Total formula weight19005.47
Authors
Meshcheryakov, V.A.,Samatey, F.A. (deposition date: 2011-06-17, release date: 2012-06-20, Last modification date: 2024-03-13)
Primary citationMeshcheryakov, V.A.,Kitao, A.,Matsunami, H.,Samatey, F.A.
Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins
Acta Crystallogr.,Sect.D, 69:812-820, 2013
Cited by
PubMed Abstract: The membrane protein FlhB is a highly conserved component of the flagellar secretion system. It is composed of an N-terminal transmembrane domain and a C-terminal cytoplasmic domain (FlhBC). Here, the crystal structures of FlhBC from Salmonella typhimurium and Aquifex aeolicus are described at 2.45 and 2.55 Å resolution, respectively. These flagellar FlhBC structures are similar to those of paralogues from the needle type III secretion system, with the major difference being in a linker that connects the transmembrane and cytoplasmic domains of FlhB. It was found that deletion of a short flexible loop in a globular part of Salmonella FlhBC leads to complete inhibition of secretion by the flagellar secretion system. Molecular-dynamics calculations demonstrate that the linker region is the most flexible part of FlhBC and that the deletion of the loop reduces this flexibility. These results are in good agreement with previous studies showing the importance of the linker in the function of FlhB and provide new insight into the relationship between the different parts of the FlhBC molecule.
PubMed: 23633590
DOI: 10.1107/S0907444913002102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.45 Å)
Structure validation

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