Making or Breaking Metal- Dependent Catalytic Activity: The Role of Stammers in Designed Three- Stranded Coiled Coils
dc.contributor.author | Pinter, Tyler B. J. | |
dc.contributor.author | Manickas, Elizabeth C. | |
dc.contributor.author | Tolbert, Audrey E. | |
dc.contributor.author | Koebke, Karl J. | |
dc.contributor.author | Deb, Aniruddha | |
dc.contributor.author | Penner‐hahn, James E. | |
dc.contributor.author | Pecoraro, Vincent L. | |
dc.date.accessioned | 2020-11-04T16:02:22Z | |
dc.date.available | WITHHELD_13_MONTHS | |
dc.date.available | 2020-11-04T16:02:22Z | |
dc.date.issued | 2020-11-09 | |
dc.identifier.citation | Pinter, Tyler B. J.; Manickas, Elizabeth C.; Tolbert, Audrey E.; Koebke, Karl J.; Deb, Aniruddha; Penner‐hahn, James E. ; Pecoraro, Vincent L. (2020). "Making or Breaking Metal- Dependent Catalytic Activity: The Role of Stammers in Designed Three- Stranded Coiled Coils." Angewandte Chemie 132(46): 20625-20629. | |
dc.identifier.issn | 0044-8249 | |
dc.identifier.issn | 1521-3757 | |
dc.identifier.uri | https://hdl.handle.net/2027.42/163477 | |
dc.description.abstract | While many life- critical reactions would be infeasibly slow without metal cofactors, a detailed understanding of how protein structure can influence catalytic activity remains elusive. Using de novo designed three- stranded coiled coils (TRI and Grand peptides formed using a heptad repeat approach), we examine how the insertion of a three residue discontinuity, known as a stammer insert, directly adjacent to a (His)3 metal binding site alters catalytic activity. The stammer, which locally alters the twist of the helix, significantly increases copper- catalyzed nitrite reductase activity (CuNiR). In contrast, the well- established zinc- catalyzed carbonic anhydrase activity (p- nitrophenyl acetate, pNPA) is effectively ablated. This study illustrates how the perturbation of the protein sequence using non- coordinating and non- acid base residues in the helical core can perturb metalloenzyme activity through the simple expedient of modifying the helical pitch adjacent to the catalytic center.The addition of a stammer discontinuity within a de novo designed three- stranded coiled coil containing a symmetric (His)3 metal binding site enhances copper nitrite reductase activity and ablates zinc esterase activity. These results suggest catalytic activity of designed α- helical systems can be modulated by inclusion of discontinuity insertions and deletions. | |
dc.publisher | Wiley Periodicals, Inc. | |
dc.publisher | ACS Publications | |
dc.subject.other | protein design | |
dc.subject.other | coiled coils | |
dc.subject.other | enzyme catalysis | |
dc.subject.other | metalloproteins | |
dc.subject.other | stammers | |
dc.title | Making or Breaking Metal- Dependent Catalytic Activity: The Role of Stammers in Designed Three- Stranded Coiled Coils | |
dc.type | Article | |
dc.rights.robots | IndexNoFollow | |
dc.subject.hlbsecondlevel | Chemical Engineering | |
dc.subject.hlbsecondlevel | Chemistry | |
dc.subject.hlbsecondlevel | Materials Science and Engineering | |
dc.subject.hlbtoplevel | Engineering | |
dc.subject.hlbtoplevel | Science | |
dc.description.peerreviewed | Peer Reviewed | |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/163477/3/ange202008356_am.pdf | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/163477/2/ange202008356-sup-0001-misc_information.pdf | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/163477/1/ange202008356.pdf | en_US |
dc.identifier.doi | 10.1002/ange.202008356 | |
dc.identifier.source | Angewandte Chemie | |
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