3dl8

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Template:STRUCTURE 3dl8

Contents 1 Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA 2 Function 3 About this Structure 4 See Also 5 Reference

Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA

Template:ABSTRACT PUBMED 18923516

Function

[SECG_AQUAE] Subunit of the protein translocation channel SecYEG. [SECA_BACSU] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity).[HAMAP-Rule:MF_01382] [SECY_AQUAE] The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity).

About this Structure

3dl8 is a 8 chain structure with sequence from Aquifex aeolicus and Bacillus subtilis. Full crystallographic information is available from OCA.

See Also

• Preprotein translocase
• SecA

Reference

• Zimmer J, Nam Y, Rapoport TA. Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature. 2008 Oct 16;455(7215):936-43. PMID:18923516 doi:10.1038/nature07335