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Literature DB >> 8357800

Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping.

Abstract

We have mapped the interface between the two transmembrane alpha-helices in the membrane domain of the Escherichia coli enzyme leader peptidase by analyzing disulfides formed between pairs of cysteine residues introduced near their respective periplasmic ends. The interface is formed primarily from aliphatic amino acids, and the two helices appear to pack against each other in a left-handed supercoil. We suggest that disulfide mapping may be a generally applicable approach for the construction of models of helix-helix interfaces in membrane proteins.

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Year: 1993 PMID： 8357800 DOI： 10.1021/bi00084a020

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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Cited

13 in total

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2. Molecular dynamics simulations of the E1/E2 transmembrane domain of the Semliki Forest virus.

Authors: Ana Caballero-Herrera; Lennart Nilsson
Journal: Biophys J Date: 2003-12 Impact factor: 4.033

3. Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane.

Authors: Sven U Heinrich; Tom A Rapoport
Journal: EMBO J Date: 2003-07-15 Impact factor: 11.598

4. Cysteine residues in the transmembrane regions of M13 procoat protein suggest that oligomeric coat proteins assemble onto phage progeny.

Authors: Christof Nagler; Gisela Nagler; Andreas Kuhn
Journal: J Bacteriol Date: 2007-01-19 Impact factor: 3.490

5. Palmitoylation, membrane-proximal basic residues, and transmembrane glycine residues in the reovirus p10 protein are essential for syncytium formation.

Authors: Maya Shmulevitz; Jayme Salsman; Roy Duncan
Journal: J Virol Date: 2003-09 Impact factor: 5.103

Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping.

1. Mapping an interface of SecY (PrlA) and SecE (PrlG) by using synthetic phenotypes and in vivo cross-linking.

2. Molecular dynamics simulations of the E1/E2 transmembrane domain of the Semliki Forest virus.

3. Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane.

4. Cysteine residues in the transmembrane regions of M13 procoat protein suggest that oligomeric coat proteins assemble onto phage progeny.

5. Palmitoylation, membrane-proximal basic residues, and transmembrane glycine residues in the reovirus p10 protein are essential for syncytium formation.

6. Position and role of the BK channel alpha subunit S0 helix inferred from disulfide crosslinking.

Review 7. The chemistry and enzymology of the type I signal peptidases.

8. Properties of a cysteine-free proton-pumping nicotinamide nucleotide transhydrogenase.

Review 9. Signal peptidase I: cleaving the way to mature proteins.

10. A small subset of signal peptidase residues are perturbed by signal peptide binding.