3CM1

Crystal structure of SsgA-like sporulation-specific cell division protein (YP_290167.1) from Thermobifida fusca YX-ER1 at 2.60 A resolution

3CM1 の概要

• エントリーDOI: 10.2210/pdb3cm1/pdb
• 分子名称: SsgA-like sporulation-specific cell division protein (1 entity in total)
• 機能のキーワード: yp_290167.1, ssga-like sporulation-specific cell division protein, streptomyces sporulation and cell division protein, ssga, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, cell cycle
• 由来する生物種: Thermobifida fusca
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 46247.68

構造登録者

Joint Center for Structural Genomics (JCSG),Chruszcz, M.,Minor, W.,Wang, S. (登録日: 2008-03-20, 公開日: 2008-04-01, 最終更新日: 2024-10-30)

主引用文献

Xu, Q.,Traag, B.A.,Willemse, J.,McMullan, D.,Miller, M.D.,Elsliger, M.A.,Abdubek, P.,Astakhova, T.,Axelrod, H.L.,Bakolitsa, C.,Carlton, D.,Chen, C.,Chiu, H.J.,Chruszcz, M.,Clayton, T.,Das, D.,Deller, M.C.,Duan, L.,Ellrott, K.,Ernst, D.,Farr, C.L.,Feuerhelm, J.,Grant, J.C.,Grzechnik, A.,Grzechnik, S.K.,Han, G.W.,Jaroszewski, L.,Jin, K.K.,Klock, H.E.,Knuth, M.W.,Kozbial, P.,Krishna, S.S.,Kumar, A.,Marciano, D.,Minor, W.,Mommaas, A.M.,Morse, A.T.,Nigoghossian, E.,Nopakun, A.,Okach, L.,Oommachen, S.,Paulsen, J.,Puckett, C.,Reyes, R.,Rife, C.L.,Sefcovic, N.,Tien, H.J.,Trame, C.B.,van den Bedem, H.,Wang, S.,Weekes, D.,Hodgson, K.O.,Wooley, J.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A.,van Wezel, G.P.
Structural and functional characterizations of SsgB, a conserved activator of developmental cell division in morphologically complex actinomycetes.
J.Biol.Chem., 284:25268-25279, 2009

PubMed Abstract: SsgA-like proteins (SALPs) are a family of homologous cell division-related proteins that occur exclusively in morphologically complex actinomycetes. We show that SsgB, a subfamily of SALPs, is the archetypal SALP that is functionally conserved in all sporulating actinomycetes. Sporulation-specific cell division of Streptomyces coelicolor ssgB mutants is restored by introduction of distant ssgB orthologues from other actinomycetes. Interestingly, the number of septa (and spores) of the complemented null mutants is dictated by the specific ssgB orthologue that is expressed. The crystal structure of the SsgB from Thermobifida fusca was determined at 2.6 A resolution and represents the first structure for this family. The structure revealed similarities to a class of eukaryotic "whirly" single-stranded DNA/RNA-binding proteins. However, the electro-negative surface of the SALPs suggests that neither SsgB nor any of the other SALPs are likely to interact with nucleotide substrates. Instead, we show that a conserved hydrophobic surface is likely to be important for SALP function and suggest that proteins are the likely binding partners.

PubMed: 19567872
DOI: 10.1074/jbc.M109.018564

実験手法

X-RAY DIFFRACTION (2.6 Å)