5L22
PrtD T1SS ABC transporter
Summary for 5L22
| Entry DOI | 10.2210/pdb5l22/pdb |
| Descriptor | ABC transporter (HlyB subfamily), ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | t1ss, abc transporter, atpase, secretion, protein transport |
| Biological source | Aquifex aeolicus (strain VF5) |
| Total number of polymer chains | 2 |
| Total formula weight | 129385.15 |
| Authors | Morgan, J.L.W.,Zimmer, J. (deposition date: 2016-07-30, release date: 2017-03-08, Last modification date: 2024-03-06) |
| Primary citation | Morgan, J.L.,Acheson, J.F.,Zimmer, J. Structure of a Type-1 Secretion System ABC Transporter. Structure, 25:522-529, 2017 Cited by PubMed Abstract: Type-1 secretion systems (T1SSs) represent a widespread mode of protein secretion across the cell envelope in Gram-negative bacteria. The T1SS is composed of an inner-membrane ABC transporter, a periplasmic membrane-fusion protein, and an outer-membrane porin. These three components assemble into a complex spanning both membranes and providing a conduit for the translocation of unfolded polypeptides. We show that ATP hydrolysis and assembly of the entire T1SS complex is necessary for protein secretion. Furthermore, we present a 3.15-Å crystal structure of AaPrtD, the ABC transporter found in the Aquifex aeolicus T1SS. The structure suggests a substrate entry window just above the transporter's nucleotide binding domains. In addition, highly kinked transmembrane helices, which frame a narrow channel not observed in canonical peptide transporters, are likely involved in substrate translocation. Overall, the AaPrtD structure supports a polypeptide transport mechanism distinct from alternating access. PubMed: 28216041DOI: 10.1016/j.str.2017.01.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
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