Bridging of partially negative atoms by hydrogen bonds from main‐chain NH groups in proteins: The crown motif |
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Authors: | David P Leader E James Milner‐White |
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Institution: | College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, United Kingdom |
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Abstract: | The backbone NH groups of proteins can form N1N3‐bridges to δ‐ve or anionic acceptor atoms when the tripeptide in which they occur orients them appropriately, as in the RL and LR nest motifs, which have dihedral angles 1,2‐αRαL and 1,2‐αLαR, respectively. We searched a protein database for structures with backbone N1N3‐bridging to anionic atoms of the polypeptide chain and found that RL and LR nests together accounted for 92% of examples found (88% RL nests, 4% LR nests). Almost all the remaining 8% of N1N3‐bridges were found within a third tripeptide motif which has not been described previously. We term this a “crown,” because of the disposition of the tripeptide CO groups relative to the three NH groups and the acceptor oxygen anion, and the crown together with its bridged anion we term a “crown bridge.” At position 2 of these structures the dihedral angles have a tight αR distribution, but at position 1 they have a wider distribution, with ? and ψ values generally being lower than those at position 1. Over half of crown bridges involve the backbone CO group three residues N‐terminal to the tripeptide, the remainder being to other main‐chain or side‐chain carbonyl groups. As with nests, bridging of crowns to oxygen atoms within ligands was observed, as was bridging to the sulfur atom of an iron‐sulfur cluster. This latter property may be of significance for protein evolution. Proteins 2015; 83:2067–2076. © 2015 Wiley Periodicals, Inc. |
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Keywords: | crown bridge protein structure protein motif peptide bond nest motif ligand |
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