1IJ1

GCN4-pVLT Coiled-coil Trimer with Threonine at the d(12) Position

Summary for 1IJ1

• Entry DOI: 10.2210/pdb1ij1/pdb
• Descriptor: GENERAL CONTROL PROTEIN GCN4, ZINC ION (3 entities in total)
• Functional Keywords: gcn4, coiled coil, transcription
• Cellular location: Nucleus: P03069
• Total number of polymer chains: 3
• Total formula weight: 12210.26

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

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: 11371197
DOI: 10.1021/bi002829w

Experimental method

X-RAY DIFFRACTION (1.86 Å)