3B1S
Crystal structure of the cytoplasmic domain of FlhB from Aquifex aeolicus
Summary for 3B1S
| Entry DOI | 10.2210/pdb3b1s/pdb |
| Related | 3B0Z |
| Descriptor | Flagellar biosynthetic protein flhB (3 entities in total) |
| Functional Keywords | flagella, type iii secretion system, protein transport, membrane protein |
| Biological source | Aquifex aeolicus More |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : O67813 O67813 |
| Total number of polymer chains | 6 |
| Total formula weight | 47499.00 |
| Authors | Meshcheryakov, V.A.,Samatey, F.A. (deposition date: 2011-07-08, release date: 2012-07-11, Last modification date: 2024-03-13) |
| Primary citation | Meshcheryakov, 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: 23633590DOI: 10.1107/S0907444913002102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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