3DRY

X-ray crystal structure of human KCTD5 protein crystallized in low-salt buffer

Summary for 3DRY

• Entry DOI: 10.2210/pdb3dry/pdb
• Related: 3DRX 3DRZ
• Descriptor: BTB/POZ domain-containing protein KCTD5 (1 entity in total)
• Functional Keywords: kctd5, btb/poz, golgi, grasp55, potassium channel domain t1, pentameric assembly, host-virus interaction, nucleus, unknown function
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol: Q9NXV2
• Total number of polymer chains: 5
• Total formula weight: 115209.77

Authors

Tereshko, V.,Dementieva, I.,Goldstein, S.A.N. (deposition date: 2008-07-11, release date: 2009-02-17, Last modification date: 2024-11-13)

Primary citation

Dementieva, I.S.,Tereshko, V.,McCrossan, Z.A.,Solomaha, E.,Araki, D.,Xu, C.,Grigorieff, N.,Goldstein, S.A.
Pentameric assembly of potassium channel tetramerization domain-containing protein 5.
J.Mol.Biol., 387:175-191, 2009

PubMed Abstract: We report the X-ray crystal structure of human potassium channel tetramerization domain-containing protein 5 (KCTD5), the first member of the family to be so characterized. Four findings were unexpected. First, the structure reveals assemblies of five subunits while tetramers were anticipated; pentameric stoichiometry is observed also in solution by scanning transmission electron microscopy mass analysis and analytical ultracentrifugation. Second, the same BTB (bric-a-brac, tramtrack, broad complex) domain surface mediates the assembly of five KCTD5 and four voltage-gated K(+) (Kv) channel subunits; four amino acid differences appear crucial. Third, KCTD5 complexes have well-defined N- and C-terminal modules separated by a flexible linker that swivels by approximately 30 degrees; the C-module shows a new fold and is required to bind Golgi reassembly stacking protein 55 with approximately 1 microM affinity, as judged by surface plasmon resonance and ultracentrifugation. Fourth, despite the homology reflected in its name, KCTD5 does not impact the operation of Kv4.2, Kv3.4, Kv2.1, or Kv1.2 channels.

PubMed: 19361449
DOI: 10.1016/j.jmb.2009.01.030

Experimental method

X-RAY DIFFRACTION (3.3 Å)