Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1PIQ

CRYSTAL STRUCTURE OF GCN4-PIQ, A TRIMERIC COILED COIL WITH BURIED POLAR RESIDUES

Summary for 1PIQ
Entry DOI10.2210/pdb1piq/pdb
DescriptorPROTEIN (GENERAL CONTROL PROTEIN GCN4-PIQ), CHLORIDE ION (3 entities in total)
Functional Keywordsion binding, buried polar residue, dna binding protein
Cellular locationNucleus: P03069
Total number of polymer chains1
Total formula weight3836.95
Authors
Eckert, D.M.,Malashkevich, V.N.,Kim, P.S. (deposition date: 1998-09-25, release date: 1998-09-30, Last modification date: 2024-10-30)
Primary citationEckert, D.M.,Malashkevich, V.N.,Kim, P.S.
Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues.
J.Mol.Biol., 284:859-865, 1998
Cited by
PubMed Abstract: Coiled coils consist of two or more alpha-helices wrapped around each other with a superhelical twist. The interfaces between helices of a coiled coil are formed by hydrophobic amino acid residues packed in a "knobs-into-holes" arrangement. Most naturally occurring coiled coils, however, also contain buried polar residues, as do the cores of the majority of naturally occurring globular proteins. Two common buried polar residues in both dimeric and trimeric coiled coils are asparagine and glutamine. In dimeric coiled coils, buried asparagine, but not glutamine, residues have been shown to confer specificity of oligomerization. We have placed a glutamine residue in the otherwise hydrophobic interior of a stable trimeric coiled coil, GCN4-pII, to study the effect of this buried polar residue in a trimeric coiled-coil environment. The resulting peptide, GCN4-pIQI, is a discrete, trimeric coiled coil with a lower stability than GCN4-pII. The crystal structure determined to 1.8 A shows that GCN4-pIQI is a trimeric coiled coil with a chloride ion coordinated by one buried glutamine residue from each monomer.
PubMed: 9837709
DOI: 10.1006/jmbi.1998.2214
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon