5hz7
From Proteopedia
High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria meningitidis in fusion with MBP
Structural highlights
FunctionMALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMedDNA transformation is a widespread process allowing bacteria to capture free DNA by using filamentous nano-machines composed of type IV pilins. These proteins can act as DNA receptors as demonstrated by the finding that Neisseria meningitidis ComP minor pilin has intrinsic DNA-binding ability. ComP binds DNA better when it contains the DNA-uptake sequence (DUS) motif abundant in this species genome, playing a role in its trademark ability to selectively take up its own DNA. Here, we report high-resolution structures for meningococcal ComP and Neisseria subflava ComPsub, which recognize different DUS motifs. We show that they are structurally identical type IV pilins that pack readily into filament models and display a unique DD region delimited by two disulfide bonds. Functional analysis of ComPsub defines a new mode of DNA binding involving the DD region, adapted for exported DNA receptors. A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.,Berry JL, Xu Y, Ward PN, Lea SM, Matthews SJ, Pelicic V Structure. 2016 May 3. pii: S0969-2126(16)30037-5. doi:, 10.1016/j.str.2016.04.001. PMID:27161979[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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