1IJ0
Coiled Coil Trimer GCN4-pVLS Ser at Buried D Position
Summary for 1IJ0
| Entry DOI | 10.2210/pdb1ij0/pdb |
| Descriptor | GENERAL CONTROL PROTEIN GCN4, ZINC ION (3 entities in total) |
| Functional Keywords | coiled coil trimer, transcription |
| Cellular location | Nucleus: P03069 |
| Total number of polymer chains | 3 |
| Total formula weight | 12168.18 |
| Authors | Akey, D.L.,Malashkevich, V.N.,Kim, P.S. (deposition date: 2001-04-24, release date: 2001-08-08, Last modification date: 2021-10-27) |
| Primary citation | Akey, D.L.,Malashkevich, V.N.,Kim, P.S. Buried polar residues in coiled-coil interfaces. Biochemistry, 40:6352-6360, 2001 Cited by PubMed Abstract: Coiled coils, estimated to constitute 3-5% of the encoded residues in most genomes, are characterized by a heptad repeat, (abcdefg)(n), where the buried a and d positions form the interface between multiple alpha-helices. Although generally hydrophobic, a substantial fraction ( approximately 20%) of these a- and d-position residues are polar or charged. We constructed variants of the well-characterized coiled coil GCN4-p1 with a single polar residue (Asn, Gln, Ser, or Thr) at either an a or a d position. The stability and oligomeric specificity of each variant were measured, and crystal structures of coiled-coil trimers with threonine or serine at either an a or a d position were determined. The structures show how single polar residues in the interface affect not only local packing, but also overall coiled-coil geometry as seen by changes in the Crick supercoil parameters and core cavity volumes. PubMed: 11371197DOI: 10.1021/bi002829w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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