1M6N
Crystal structure of the SecA translocation ATPase from Bacillus subtilis
Summary for 1M6N
| Entry DOI | 10.2210/pdb1m6n/pdb |
| Related | 1M74 |
| Descriptor | Preprotein translocase secA, SULFATE ION (3 entities in total) |
| Functional Keywords | protein translocation; atpase; transmembrane transport; helicase family structure; mechanochemisty, protein transport |
| Biological source | Bacillus subtilis |
| Cellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P28366 |
| Total number of polymer chains | 1 |
| Total formula weight | 92066.20 |
| Authors | Hunt, J.F.,Weinkauf, S.,Henry, L.,Fak, J.J.,McNicholas, P.,Oliver, D.B.,Deisenhofer, J. (deposition date: 2002-07-16, release date: 2002-09-20, Last modification date: 2024-02-14) |
| Primary citation | Hunt, J.F.,Weinkauf, S.,Henry, L.,Fak, J.J.,McNicholas, P.,Oliver, D.B.,Deisenhofer, J. Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA Science, 297:2018-2026, 2002 Cited by PubMed Abstract: The SecA adenosine triphosphatase (ATPase) mediates extrusion of the amino termini of secreted proteins from the eubacterial cytosol based on cycles of reversible binding to the SecYEG translocon. We have determined the crystal structure of SecA with and without magnesium-adenosine diphosphate bound to the high-affinity ATPase site at 3.0 and 2.7 angstrom resolution, respectively. Candidate sites for preprotein binding are located on a surface containing the SecA epitopes exposed to the periplasm upon binding to SecYEG and are thus positioned to deliver preprotein to SecYEG. Comparisons with structurally related ATPases, including superfamily I and II ATP-dependent helicases, suggest that the interaction geometry of the tandem motor domains in SecA is modulated by nucleotide binding, which is shown by fluorescence anisotropy experiments to reverse an endothermic domain-dissociation reaction hypothesized to gate binding to SecYEG. PubMed: 12242434DOI: 10.1126/science.1074424 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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