3CM1

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

Summary for 3CM1

• Entry DOI: 10.2210/pdb3cm1/pdb
• Descriptor: SsgA-like sporulation-specific cell division protein (1 entity in total)
• Functional Keywords: 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
• Biological source: Thermobifida fusca
• Total number of polymer chains: 3
• Total formula weight: 46247.68

Authors

Joint Center for Structural Genomics (JCSG),Chruszcz, M.,Minor, W.,Wang, S. (deposition date: 2008-03-20, release date: 2008-04-01, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)