Selective photoaffinity labeling identifies the signal peptide binding domain on SecA.

No abstract is available for this paper.

• Publication year

  2007

• Venue

  Journal of Molecular Biology

• Publication date

  2007-01-19

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.JMB.2006.10.027PMID 17084862PMCID PMC1851904
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• The Conformation of a Signal Peptide Bound by Escherichia coli Preprotein Translocase SecA*

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• Protein translocation by the Sec61/SecY channel.

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• Identification of the Preprotein Binding Domain of SecA*

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• Probing the affinity of SecA for signal peptide in different environments.

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• Demonstration of a specific Escherichia coli SecY-signal peptide interaction.

  2004cited by this paper
• A large conformational change of the translocation ATPase SecA.

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• Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study.

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• Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

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• Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin

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• Nucleotide and phospholipid-dependent control of PPXD and C-domain association for SecA ATPase.

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• Crystal Structure of M. tuberculosis SecA, A Preprotein Translocating ATPase

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• The ATPase domain of SecA can form a tetramer in solution.

  2002cited by this paper
• Allosteric Communication between Signal Peptides and the SecA Protein DEAD Motor ATPase Domain*

  2002cited by this paper
• SecA specificity for different signal peptides.

  2002cited by this paper
• Calmodulin in action: diversity in target recognition and activation mechanisms.

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• Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA

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  2001cited by this paper
• Cross‐talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function

  2001cited by this paper
• Effects of lipids on the interaction of SecA with model membranes.

  2001cited by this paper
• Effect of divalent cations on the ATPase activity of Escherichia coli SecA

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• The high affinity ATP binding site modulates the SecA–precursor interaction

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• Signal Peptide Determinants of SecA Binding and Stimulation of ATPase Activity*

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