PDB ID or protein name

1tf5 » Translocation ATPase SecA

1tf5 » Translocation ATPase SecA
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Topology in Bacterial Gram-positive plasma membrane
Topologyout side
in side
1tf5 » Translocation ATPase SecA
Depth 2.5 ± 1.1 Å
Tilt Angle 64 ± 5°
ΔGtransfer -7.0 kcal/mol
Links to 1tf5 PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology in
Resolution 2.1 Å
Other PDB entries representing this structure 1m6n, 1m74, 1tf2
Number of subunits 1
Experimental Verification for 1tf5 » Translocation ATPase SecA
Interacts with lipid bilayers in monomeric state (1tf2, 1tf5) and undergoes significant conformational changes (Osborne et al. 2004). The structure of dimer (1m74, 1m6n) is different. More data on iteractions of SecA from E.coli with membranes and SecY: van Dalen and de Kruijff (2004), Breukink et al. (1992), Dapic and Oliver (2000).
4 references
Breukink E, Demel RA, de Korte-Kool G, de Kruijff B. 1992. SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study. Biochemistry. 31: 1119-1124. PubMed
Dapic V, Oliver D. 2000. Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase. J Biol Chem. 275: 25000-25007. PubMed
Osborne AR, Clemons WM Jr, Rapoport TA. 2004. A large conformational change of the translocation ATPase SecA. Proc Natl Acad Sci U S A. 101:10937-42. PubMed
van Dalen A, de Kruijff B. 2004. The role of lipids in membrane insertion and translocation of bacterial proteins. Biochim Biophys Acta. 1694: 97-109. PubMed
Comments on 1tf5 » Translocation ATPase SecA
Part of the prokaryotic protein translocation apparatus which comprise secA, secB, secD, secE, secF, secG and secY. SecA has a central role in coupling the hydrolysis of ATP to the transfer of pre-secretory proteins across the membrane.