2fsg: Difference between revisions

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{{STRUCTURE_2fsg|  PDB=2fsg  |  SCENE=  }}  
{{STRUCTURE_2fsg|  PDB=2fsg  |  SCENE=  }}  


'''Complex SecA:ATP from Escherichia coli'''
===Complex SecA:ATP from Escherichia coli===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17229438 17229438]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17229438 17229438]
Escherichia coli SecA truncated at its termini is functional and dimeric., Karamanou S, Sianidis G, Gouridis G, Pozidis C, Papanikolau Y, Papanikou E, Economou A, FEBS Lett. 2005 Feb 14;579(5):1267-71. Epub 2005 Jan 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15710424 15710424]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Protein translocation]]
[[Category: Protein translocation]]
[[Category: Seca]]
[[Category: Seca]]
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