Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin. Export

@article{citeulike:2492278, abstract = {An invariant substructure that forms two interlocked pairs of neighboring beta-strands occurs in essentially all known sandwich-like proteins. Eight conserved positions in these strands were recently shown to act as structural determinants. To test whether the residues at these invariant positions are conserved for mechanistic (i.e., part of folding nucleus) or energetic (i.e., governing native-state stability) reasons, we characterized the folding behavior of eight point-mutated variants of the sandwich-like protein Pseudomonas aeruginosa apo-azurin. We find a simple relationship among the conserved positions: half of the residues form native-like interactions in the folding transition state, whereas the others do not participate in the folding nucleus but govern high native-state stability. Thus, evolutionary preservation of these specific positions gives both mechanistic and energetic advantages to members of the sandwich-like protein family.}, address = {Department of Biochemistry and Cell Biology, Keck Center for Structural Computational Biology, Rice University, 6100 Main Street, Houston, TX 77251, USA.}, author = {Wilson, C. J. and Wittung-Stafshede, P.}, citeulike-article-id = {2492278}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0501038102}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/15753320}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=15753320}, day = {15}, doi = {10.1073/pnas.0501038102}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {folding-nucleus, protein-stability}, month = {March}, number = {11}, pages = {3984--3987}, posted-at = {2008-03-09 03:38:30}, priority = {0}, title = {Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin.}, url = {http://dx.doi.org/10.1073/pnas.0501038102}, volume = {102}, year = {2005} }

TY - JOUR ID - citeulike:2492278 L3 - citeulike-article-id:2492278 N2 - An invariant substructure that forms two interlocked pairs of neighboring beta-strands occurs in essentially all known sandwich-like proteins. Eight conserved positions in these strands were recently shown to act as structural determinants. To test whether the residues at these invariant positions are conserved for mechanistic (i.e., part of folding nucleus) or energetic (i.e., governing native-state stability) reasons, we characterized the folding behavior of eight point-mutated variants of the sandwich-like protein Pseudomonas aeruginosa apo-azurin. We find a simple relationship among the conserved positions: half of the residues form native-like interactions in the folding transition state, whereas the others do not participate in the folding nucleus but govern high native-state stability. Thus, evolutionary preservation of these specific positions gives both mechanistic and energetic advantages to members of the sandwich-like protein family. IS - 11 JF - Proc Natl Acad Sci U S A SN - 0027-8424 AD - Department of Biochemistry and Cell Biology, Keck Center for Structural Computational Biology, Rice University, 6100 Main Street, Houston, TX 77251, USA. EP - 3987 TI - Role of structural determinants in folding of the sandwich-like protein Pseudomonas aeruginosa azurin. VL - 102 SP - 3984 KW - folding-nucleus KW - protein-stability AU - Wilson, CJ AU - Wittung-Stafshede, P PY - 2005/03/15/ UR - http://dx.doi.org/10.1073/pnas.0501038102 ER -