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3dl8
From Proteopedia
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| - | [[Image:3dl8.png|left|200px]] | ||
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{{STRUCTURE_3dl8| PDB=3dl8 | SCENE= }} | {{STRUCTURE_3dl8| PDB=3dl8 | SCENE= }} | ||
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===Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA=== | ===Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA=== | ||
| + | {{ABSTRACT_PUBMED_18923516}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/SECG_AQUAE SECG_AQUAE]] Subunit of the protein translocation channel SecYEG. [[http://www.uniprot.org/uniprot/SECA_BACSU 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] [[http://www.uniprot.org/uniprot/SECY_AQUAE 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== | ==About this Structure== | ||
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==See Also== | ==See Also== | ||
| + | *[[Preprotein translocase|Preprotein translocase]] | ||
*[[SecA|SecA]] | *[[SecA|SecA]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:018923516</ref><references group="xtra"/> | + | <ref group="xtra">PMID:018923516</ref><references group="xtra"/><references/> |
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
Revision as of 06:54, 29 September 2013
Contents |
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
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
Categories: Aquifex aeolicus | Bacillus subtilis | Nam, Y. | Rapoport, T A. | Zimmer, J. | Atp-binding | Cell membrane | Membrane | Metal-binding | Nucleotide-binding | Protein transport | Reca-type atpase membrane protein translocation protein-protein complex | Translocation | Transmembrane | Transport
