Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 56, Issue 2, Pages 298-309Publisher
WILEY
DOI: 10.1002/prot.20101
Keywords
protein structure motif; structural bioinformatics; pectate lyase; Ni-Fe hydrogenase; opine dehydrogenase; glucoamylase; xylanase; ribonuclease H; DNA polymerase; ribotoxin; phage gene 3 protein
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Funding
- NIGMS NIH HHS [GM-61302, GM-15000] Funding Source: Medline
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A new motif of three-dimensional (3D) protein structure is described, called the cisPro touch-turn. In this four-residue, three-peptide motif, the central peptide is cis. Residue 2, which precedes the proline, has phi, psi values either in the prePro region of the Ramachandran plot near -130degrees, 75degrees or in the La region near +60degrees, +60degrees. The Calpha(1)-Calpha(4) distance is 4-5 Angstrom and the two flanking peptides lie parallel to one another, making van der Waals contact rather than a hydrogen bond. Apparently, this arrangement is locally unfavorable and therefore rare, usually occurring only if needed for biological function. Of the 12 examples in a 500-protein database, cis-Pro touch-turns are found at the catalytic sites of pectate lyase, Ni-Fe hydrogenase, glucoamylase, xylanase, and opine dehydrogenase and at the primary binding sites of ribonuclease H, type I DNA polymerase, ribotoxin, and phage gene 3 protein. In each of these protein families, the touch-turns serve different roles; their functional importance is supported by conservation and mutagenesis data. In analyzing the conservation patterns of these 3D motifs, new methods for in-depth quality evaluation of the structural bioinformatic data are employed to distinguish between significant exceptions and errors. (C) 2004 Wiley-Liss, Inc.
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