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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,
Journal of Biological Chemistry (2009) 284:25268-79 PublishedPSI:Phase 2  
Joint Center for Structural GenomicsMidwest Center for Structural Genomics

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SsgA-like proteins (SALPs) are a family of homologous cell division-related proteins that occur exclusively in morphologically complex actinomycetes. ...
metabolism chemistry methods physiology 
Binding Sites Crystallography, X-Ray Amino Acid Sequence Molecular Sequence Data Escherichia coli Sequence Homology, Amino Acid Bacterial Proteins Mutation Cryoelectron Microscopy Cell Division Microscopy, Fluorescence Genetic Complementation Test Actinobacteria Microscopy, Phase-Contrast Spores, Bacterial 
19567872  
10.1074/jbc.M109.018564  
17 (Last update: 08/11/2018 11:39:01am)  
3CM1  
structure