2fsg: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:2fsg.jpg|left|200px]] | [[Image:2fsg.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2fsg", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_2fsg| PDB=2fsg | SCENE= }} | |||
}} | |||
'''Complex SecA:ATP from Escherichia coli''' | '''Complex SecA:ATP from Escherichia coli''' | ||
Line 28: | Line 25: | ||
[[Category: Papanikolau, Y.]] | [[Category: Papanikolau, Y.]] | ||
[[Category: Petratos, K.]] | [[Category: Petratos, K.]] | ||
[[Category: | [[Category: Atpase]] | ||
[[Category: | [[Category: Dna-rna helicase]] | ||
[[Category: | [[Category: Protein translocation]] | ||
[[Category: | [[Category: Seca]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:15:33 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 04:15, 4 May 2008
Complex SecA:ATP from Escherichia coli
OverviewOverview
SecA is the preprotein translocase ATPase subunit and a superfamily 2 (SF2) RNA helicase. Here we present the 2 A crystal structures of the Escherichia coli SecA homodimer in the apo form and in complex with ATP, ADP and adenosine 5'-[beta,gamma-imido]triphosphate (AMP-PNP). Each monomer contains the SF2 ATPase core (DEAD motor) built of two domains (nucleotide binding domain, NBD and intramolecular regulator of ATPase 2, IRA2), the preprotein binding domain (PBD), which is inserted in NBD and a carboxy-terminal domain (C-domain) linked to IRA2. The structures of the nucleotide complexes of SecA identify an interfacial nucleotide-binding cleft located between the two DEAD motor domains and residues critical for ATP catalysis. The dimer comprises two virtually identical protomers associating in an antiparallel fashion. Dimerization is mediated solely through extensive contacts of the DEAD motor domains leaving the C-domain facing outwards from the dimerization core. This dimerization mode explains the effect of functionally important mutations and is completely different from the dimerization models proposed for other SecA structures. The repercussion of these findings on translocase assembly and catalysis is discussed.
About this StructureAbout this Structure
2FSG is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structure of dimeric SecA, the Escherichia coli preprotein translocase motor., Papanikolau Y, Papadovasilaki M, Ravelli RB, McCarthy AA, Cusack S, Economou A, Petratos K, J Mol Biol. 2007 Mar 9;366(5):1545-57. Epub 2006 Dec 23. PMID:17229438 Page seeded by OCA on Sun May 4 04:15:33 2008