3cm1
Crystal structure of SsgA-like sporulation-specific cell division protein (YP_290167.1) from Thermobifida fusca YX-ER1 at 2.60 A resolution
Structural highlights
FunctionSSGB_THEFY Involved in sporulation-specific cell division (PubMed:19567872). Required for early stages of sporulation. Important in the process of growth cessation prior to sporulation-specific cell division. Recruits cell division protein FtsZ to the future septum sites and tethers the contractile ring structure (Z ring) to the cytoplasmic membrane during sporulation (By similarity). Stimulates polymerization and filament length of FtsZ in vitro (PubMed:21205868).[UniProtKB:Q9L268][1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSsgA-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. Structural and functional characterizations of SsgB, a conserved activator of developmental cell division in morphologically complex actinomycetes.,Xu Q, Traag BA, Willemse J, McMullan D, Miller MD, Elsliger MA, Abdubek P, Astakhova T, Axelrod HL, Bakolitsa C, Carlton D, Chen C, Chiu HJ, Chruszcz M, Clayton T, Das D, Deller MC, Duan L, Ellrott K, Ernst D, Farr CL, Feuerhelm J, Grant JC, Grzechnik A, Grzechnik SK, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Krishna SS, Kumar A, Marciano D, Minor W, Mommaas AM, Morse AT, Nigoghossian E, Nopakun A, Okach L, Oommachen S, Paulsen J, Puckett C, Reyes R, Rife CL, Sefcovic N, Tien HJ, Trame CB, van den Bedem H, Wang S, Weekes D, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA, van Wezel GP J Biol Chem. 2009 Sep 11;284(37):25268-79. Epub 2009 Jun 30. PMID:19567872[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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