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• W1495600170 abstract "Abstract The 85-residue structure of Chromatium high potential iron protein (HiPIP) has been determined by x-ray diffraction methods at 2.0 A resolution, and is currently undergoing crystallographic refinement. The partially refined HiPIP structure reported here has an R factor of 0.24. Moreover, bond distances and angles have been constrained to their expected values, so that a model may be constructed from standard brass parts. Thus, it is an unusually well determined protein structure. The Fe4S*4 cluster (Carter, C. W., Jr., Freer, S. T., Xuong, Ng. H., Alden, R. A., and Kraut, J. (1971) Cold Spring Harbor Symp. Quant. Biol. 36, 381–385) is covalently attached to the protein by Fe—S bonds at cysteine residues 43, 46, 63, and 77. Residues 1–42 fold up upon this cluster binding segment. Most of the interface between these NH2- and COOH-terminal segments consists of packed nonpolar side chains. The chain segment containing Cys 77 is trapped inside this interface where it forms a stretch of antiparallel β sheet with residues 17–20 in the NH2-terminal half of the chain. This unusual architecture probably accounts for the relatively high stability of HiPIP (Dus, K., DeKlerk, H., Sletten, K., and Bartsch, R. G. (1967) Biochim. Biophys. Acta 140, 291–311). The Tyr 19 side chain abuts the Fe4S*4 cluster in a manner similar to that observed for Tyr 2 and Tyr 28 in Peptococcus aerogenes ferredoxin (Adman, E. T., Sieker, L. C., and Jensen, L. H. (1973) J. Biol. Chem. 248, 3987–3996). The polypeptide chain conformation may be described, almost in its entirety, as a sequence of α helical or extended conformations and hairpin turns. Moreover, most of these secondary structures are surprisingly close in their detailed geometry to those predicted to be of lowest energy. More than 75% of the main chain hydrogen bonding sites are bonded either within secondary structures (47%) or to water (30%). Thus these bonds may be formed prior to complete assembly of the entire structure. Hairpin turns are conspicuously associated with the protein-water interface: they contain a large majority of the polar side chains and their main chain carbonyl oxygen and amido nitrogen atoms bind a disproportionately large fraction of the fixed water molecules. Sequence-structure correlations of the type proposed by Robson and Pain (Robson, B., and Pain, R. H. (1971) J. Mol. Biol. 58, 237–259) and Lewis et al. (Lewis, P. N., Momany, F. A., and Scheraga, H. A. (1971) Proc. Nat. Acad. Sci. U. S. A. 68, 2293–2297) turn out to be quite accurate, and the most serious discrepancy between predicted and observed structures can be rationalized convincingly in terms of Fe4S*4 cluster binding requirements. These observations appear to weigh heavily against theories of protein folding which involve early, nonspecific micelle formation (Robson, B., and Pain, R. H. (1971) J. Mol. Biol. 58, 237–259)." @default.
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• W1495600170 date "1974-07-01" @default.
• W1495600170 modified "2023-10-16" @default.
• W1495600170 title "Two-Angstrom Crystal Structure of Oxidized Chromatium High Potential Iron Protein" @default.
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• W1495600170 cites W1554521867 @default.
• W1495600170 cites W1570569542 @default.
• W1495600170 cites W1965543507 @default.
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• W1495600170 cites W1988211700 @default.
• W1495600170 cites W1990544999 @default.
• W1495600170 cites W1991618721 @default.
• W1495600170 cites W1992925611 @default.
• W1495600170 cites W2001559032 @default.
• W1495600170 cites W2004360551 @default.
• W1495600170 cites W2006540154 @default.
• W1495600170 cites W2013653287 @default.
• W1495600170 cites W2014694459 @default.
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• W1495600170 cites W2028227377 @default.
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• W1495600170 cites W2036446927 @default.
• W1495600170 cites W2038147123 @default.
• W1495600170 cites W2038764332 @default.
• W1495600170 cites W2040946407 @default.
• W1495600170 cites W2047391885 @default.
• W1495600170 cites W2047915087 @default.
• W1495600170 cites W2055118532 @default.
• W1495600170 cites W2056146752 @default.
• W1495600170 cites W2059567258 @default.
• W1495600170 cites W2068399942 @default.
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• W1495600170 doi "https://doi.org/10.1016/s0021-9258(19)42505-2" @default.
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