Topological chirality of iron-sulfur proteins

Liang, Chengzhi; Mislow, Kurt

doi:10.1002/(sici)1097-0282(19971005)42:4<411::aid-bip4>3.0.co;2-t

Biopolymers

1997

DOI: 10.1002/(sici)1097-0282(19971005)42:4<411::aid-bip4>3.0.co;2-t

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Topological chirality of iron-sulfur proteins

Chengzhi Liang

Kurt Mislow

Abstract: An examination of x‐ray structures of single‐cluster [4Fe‐4S] proteins in the Protein Data Bank has revealed that all redox proteins and the glutamine 5‐phosphoribosyl‐1‐pyrophosphate amidotransferase from Bacillus subtilis have a topological configuration arbitrarily designated as D, whereas the DNA repair enzyme endonuclease III from Escherichia coli has the opposite topological configuration, L. This is the first example in which both senses of topological chirality have been observed in a class of proteins… Show more

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Cited by 2 publications

References 25 publications

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Interactions of human ribosomal protein S3 with intact and damaged DNA

et al. 2008

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Prefractionation procedures not only aid in reducing sample complexity, but also permit loading of higher protein amounts within the separation range applied to two-dimensional electrophoresis (2-DE) gels and thus facilitate the detection of less abundant protein species. Hence we developed a simple, cheap, and fast prefractionation procedure based on flat-bed isoelectric focusing (IEF) in granulated Sephadex gels, containing chaotropes, zwitterionic detergents and carrier ampholytes. After IEF, up to ten Sephadex gel fractions alongside the pH gradient are obtained, and then applied directly onto the surface of the corresponding narrow pH range immobilized pH gradient (IPG) strips as first dimension of 2-DE. The major advantages of this technology are the highly efficient electrophoretic transfer of the prefractionated proteins from the Sephadex IEF fraction into the IPG strip without any sample dilution, and full compatibility with subsequent 2-DE, because the prefractionated samples have not to be eluted, concentrated or desalted, nor does the amount of the carrier ampholytes in the Sephadex fraction interfere with IEF in IPG strips. This sample prefractionation method has been successfully applied for the separation, detection and identification of low abundance proteins from pro- and eukaryotic samples.

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Interactions of human ribosomal protein S3 with intact and damaged DNA

et al. 2008

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Energetic Selection of Topology in Ferredoxins

et al. 2012

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Models of early protein evolution posit the existence of short peptides that bound metals and ions and served as transporters, membranes or catalysts. The Cys-X-X-Cys-X-X-Cys heptapeptide located within bacterial ferredoxins, enclosing an Fe 4 S 4 metal center, is an attractive candidate for such an early peptide. Ferredoxins are ancient proteins and the simple α+β fold is found alone or as a domain in larger proteins throughout all three kingdoms of life. Previous analyses of the heptapeptide conformation in experimentally determined ferredoxin structures revealed a pervasive right-handed topology, despite the fact that the Fe 4 S 4 cluster is achiral. Conformational enumeration of a model CGGCGGC heptapeptide bound to a cubane iron-sulfur cluster indicates both left-handed and right-handed folds could exist and have comparable stabilities. However, only the natural ferredoxin topology provides a significant network of backbone-to-cluster hydrogen bonds that would stabilize the metal-peptide complex. The optimal peptide configuration (alternating α L ,α R ) is that of an α-sheet, providing an additional mechanism where oligomerization could stabilize the peptide and facilitate iron-sulfur cluster binding.

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Topological chirality of iron-sulfur proteins

Cited by 2 publications

References 25 publications

Interactions of human ribosomal protein S3 with intact and damaged DNA

Interactions of human ribosomal protein S3 with intact and damaged DNA

Energetic Selection of Topology in Ferredoxins

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