Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 387, Issue 1, Pages 175-191Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.01.030
Keywords
KCTD5; BTB; Kv channel; T1 domain; GRASP55
Categories
Funding
- US Department of Energy
- Office of Basic Energy Sciences [AC02-06CH11357]
- National Cancer Institute [YI-CO-1020]
- General Medical Science [Y1-GM-1104]
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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 similar to 30 degrees; the C-module shows a new fold and is required to bind Golgi reassembly stacking protein 55 with similar to 1 mu M 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. (C) 2009 Elsevier Ltd. All rights reserved.
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