2N9V
Solution NMR Structure of the membrane localization domain from Pasteurella multocida toxin
Summary for 2N9V
| Entry DOI | 10.2210/pdb2n9v/pdb |
| Related | 2N9W |
| NMR Information | BMRB: 18565 |
| Descriptor | Dermonecrotic toxin (1 entity in total) |
| Functional Keywords | bacterial toxin, membrane localization domains, toxin |
| Biological source | Pasteurella multocida |
| Cellular location | Cytoplasm : P17452 |
| Total number of polymer chains | 1 |
| Total formula weight | 10532.07 |
| Authors | Hisao, G.S.,Brothers, M.C.,Ho, M.,Wilson, B.A.,Rienstra, C.M. (deposition date: 2015-12-12, release date: 2016-12-07, Last modification date: 2024-05-15) |
| Primary citation | Hisao, G.S.,Brothers, M.C.,Ho, M.,Wilson, B.A.,Rienstra, C.M. The membrane localization domains of two distinct bacterial toxins form a 4-helix-bundle in solution. Protein Sci., 26:497-504, 2017 Cited by PubMed Abstract: Membrane localization domain (MLD) was first proposed for a 4-helix-bundle motif in the crystal structure of the C1 domain of Pasteurella multocida toxin (PMT). This structure motif is also found in the crystal structures of several clostridial glycosylating toxins (TcdA, TcdB, TcsL, and TcnA). The Ras/Rap1-specific endopeptidase (RRSP) module of the multifunctional autoprocessing repeats-in-toxins (MARTX) toxin produced by Vibrio vulnificus has sequence homology to the C1-C2 domains of PMT, including a putative MLD. We have determined the solution structure for the MLDs in PMT and in RRSP using solution state NMR. We conclude that the MLDs in these two toxins assume a 4-helix-bundle structure in solution. PubMed: 27977897DOI: 10.1002/pro.3097 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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