5KCI

Crystal Structure of HTC1

Summary for 5KCI

• Entry DOI: 10.2210/pdb5kci/pdb
• Descriptor: Uncharacterized protein YPL067C, ZINC ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: histidine triad amyloid toxicity, unknown function
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 23148.54

Authors

Martin, R.M.,Horowitz, S.,Koepnick, B.,Cooper, S.,Flatten, J.,Rogawski, D.S.,Koropatkin, N.M.,Beinlich, F.R.M.,Players, F.,Students, U.M.,Popovic, Z.,Baker, D.,Khatib, F.,Bardwell, J.C.A. (deposition date: 2016-06-06, release date: 2016-09-21, Last modification date: 2024-03-06)

Primary citation

Horowitz, S.,Koepnick, B.,Martin, R.,Tymieniecki, A.,Winburn, A.A.,Cooper, S.,Flatten, J.,Rogawski, D.S.,Koropatkin, N.M.,Hailu, T.T.,Jain, N.,Koldewey, P.,Ahlstrom, L.S.,Chapman, M.R.,Sikkema, A.P.,Skiba, M.A.,Maloney, F.P.,Beinlich, F.R.,Popovic, Z.,Baker, D.,Khatib, F.,Bardwell, J.C.
Determining crystal structures through crowdsourcing and coursework.
Nat Commun, 7:12549-12549, 2016

PubMed Abstract: We show here that computer game players can build high-quality crystal structures. Introduction of a new feature into the computer game Foldit allows players to build and real-space refine structures into electron density maps. To assess the usefulness of this feature, we held a crystallographic model-building competition between trained crystallographers, undergraduate students, Foldit players and automatic model-building algorithms. After removal of disordered residues, a team of Foldit players achieved the most accurate structure. Analysing the target protein of the competition, YPL067C, uncovered a new family of histidine triad proteins apparently involved in the prevention of amyloid toxicity. From this study, we conclude that crystallographers can utilize crowdsourcing to interpret electron density information and to produce structure solutions of the highest quality.

PubMed: 27633552
DOI: 10.1038/ncomms12549

Experimental method

X-RAY DIFFRACTION (1.833 Å)