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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 physiology methods 
Crystallography, X-Ray Microscopy, Fluorescence Mutation Escherichia coli Cell Division Molecular Sequence Data Microscopy, Phase-Contrast Binding Sites Cryoelectron Microscopy Amino Acid Sequence Actinobacteria Sequence Homology, Amino Acid Spores, Bacterial Bacterial Proteins Genetic Complementation Test 
19567872  
10.1074/jbc.M109.018564  
16 (Last update: 09/16/2017 11:11:29am)  
3CM1  
structure