1SNA
An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein
Summary for 1SNA
| Entry DOI | 10.2210/pdb1sna/pdb |
| Related | 1SN9 1SNE |
| Descriptor | tetrameric beta-beta-alpha mini-protein, ISOPROPYL ALCOHOL (3 entities in total) |
| Functional Keywords | protein design, domain swapping, mini-protein, oligomerization, de novo protein |
| Total number of polymer chains | 4 |
| Total formula weight | 10727.65 |
| Authors | Ali, M.H.,Peisach, E.,Allen, K.N.,Imperiali, B. (deposition date: 2004-03-10, release date: 2004-08-17, Last modification date: 2024-05-08) |
| Primary citation | Ali, M.H.,Peisach, E.,Allen, K.N.,Imperiali, B. X-ray structure analysis of a designed oligomeric miniprotein reveals a discrete quaternary architecture. Proc.Natl.Acad.Sci.Usa, 101:12183-12188, 2004 Cited by PubMed Abstract: The x-ray crystal structure of an oligomeric miniprotein has been determined to a 1.2-A resolution by means of multiwavelength anomalous diffraction phasing with selenomethionine analogs that retain the biophysical characteristics of the native peptide. Peptide 1, comprising alpha and beta secondary structure elements with only 21 aa per monomer, associates as a discrete tetramer. The peptide adopts a previously uncharacterized quaternary structure in which alpha and beta components interact to form a tightly packed and well defined hydrophobic core. The structure provides insight into the origins of the unusual thermal stability of the oligomer. The miniprotein shares many characteristics of larger proteins, including cooperative folding, lack of 1-anilino-8-naphthalene sulfonate binding, and limited deuterium exchange, and possesses a buried surface area typical of native proteins. PubMed: 15302930DOI: 10.1073/pnas.0401245101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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