Chaperone protein ClpB

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== Structural highlights ==
== Structural highlights ==
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The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, first nucleotide-binding domain <scene name='91/916397/Cv/4'>(NBD1)</scene>, a long coiled-coil <scene name='91/916397/Cv/5'>linker</scene> domain, a <scene name='91/916397/Cv/6'>second NBD</scene> and a <scene name='91/916397/Cv/7'>D2 small domain</scene>. The <scene name='91/916397/Cv/8'>first nucleotide AMPPNP binding site</scene> at NBD1 includes several hydrophobic residues as does the second NBD<ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.
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The 3D structure of ClpB trimeric complex with the nucleotide AMPPNP shows the chaperone to be comprised of several domains: <scene name='91/916397/Cv/3'>N-terminal</scene>, first nucleotide-binding domain <scene name='91/916397/Cv/4'>(NBD1)</scene>, a long coiled-coil <scene name='91/916397/Cv/5'>linker</scene> domain, a <scene name='91/916397/Cv/6'>second NBD</scene> and a <scene name='91/916397/Cv/7'>D2 small domain</scene>. The <scene name='91/916397/Cv/8'>first nucleotide AMPPNP binding site</scene> at NBD1 includes several hydrophobic residues as does the <scene name='91/916397/Cv/9'>second NBD</scene><ref>PMID:14567920</ref>. The long coiled-coil segments are implicated in the desaggregase activity of ClpB via their ability to move in opposite directions between subunits generating the mechanical force needed.
==ClpB 3D structures==
==ClpB 3D structures==

Revision as of 13:00, 7 July 2022

Thermus thermophilus ClpB complex with AMPPNP (PDB ID 1qvr)

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References

  1. ↑ Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I, Kopp J, Mogk A, Bukau B, Saibil HR. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife. 2014 Apr 30;3:e02481. doi: 10.7554/eLife.02481. PMID:24843029
  2. ↑ Wortmann SB, Wevers RA. CLPB Deficiency PMID:27891836
  3. ↑ Wortmann SB, Zietkiewicz S, Kousi M, Szklarczyk R, Haack TB, Gersting SW, Muntau AC, Rakovic A, Renkema GH, Rodenburg RJ, Strom TM, Meitinger T, Rubio-Gozalbo ME, Chrusciel E, Distelmaier F, Golzio C, Jansen JH, van Karnebeek C, Lillquist Y, Lucke T, Ounap K, Zordania R, Yaplito-Lee J, van Bokhoven H, Spelbrink JN, Vaz FM, Pras-Raves M, Ploski R, Pronicka E, Klein C, Willemsen MA, de Brouwer AP, Prokisch H, Katsanis N, Wevers RA. CLPB mutations cause 3-methylglutaconic aciduria, progressive brain atrophy, intellectual disability, congenital neutropenia, cataracts, movement disorder. Am J Hum Genet. 2015 Feb 5;96(2):245-57. doi: 10.1016/j.ajhg.2014.12.013. Epub, 2015 Jan 15. PMID:25597510 doi:http://dx.doi.org/10.1016/j.ajhg.2014.12.013
  4. ↑ Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FT. The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell. 2003 Oct 17;115(2):229-40. PMID:14567920

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