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5D4Z

Crystal structure of Repressor from Salmonella-temperate phage

Summary for 5D4Z
Entry DOI10.2210/pdb5d4z/pdb
Related5D50
DescriptorRepressor (2 entities in total)
Functional Keywordsrepressor, dna binding protein
Biological sourceSalmonella phage SPC32H
Total number of polymer chains32
Total formula weight376304.70
Authors
Kim, H.J.,Yoon, H.J.,Ryu, S.,Lee, H.H. (deposition date: 2015-08-10, release date: 2016-04-27, Last modification date: 2023-11-08)
Primary citationKim, M.,Kim, H.J.,Son, S.H.,Yoon, H.J.,Lim, Y.,Lee, J.W.,Seok, Y.-J.,Jin, K.S.,Yu, Y.G.,Kim, S.K.,Ryu, S.,Lee, H.H.
Noncanonical DNA-binding mode of repressor and its disassembly by antirepressor
Proc.Natl.Acad.Sci.USA, 113:E2480-E2488, 2016
Cited by
PubMed Abstract: DNA-binding repressors are involved in transcriptional repression in many organisms. Disabling a repressor is a crucial step in activating expression of desired genes. Thus, several mechanisms have been identified for the removal of a stably bound repressor (Rep) from the operator. Here, we describe an uncharacterized mechanism of noncanonical DNA binding and induction by a Rep from the temperate Salmonella phage SPC32H; this mechanism was revealed using the crystal structures of homotetrameric Rep (92-198) and a hetero-octameric complex between the Rep and its antirepressor (Ant). The canonical method of inactivating a repressor is through the competitive binding of the antirepressor to the operator-binding site of the repressor; however, these studies revealed several noncanonical features. First, Ant does not compete for the DNA-binding region of Rep. Instead, the tetrameric Ant binds to the C-terminal domains of two asymmetric Rep dimers. Simultaneously, Ant facilitates the binding of the Rep N-terminal domains to Ant, resulting in the release of two Rep dimers from the bound DNA. Second, the dimer pairs of the N-terminal DNA-binding domains originate from different dimers of a Rep tetramer (trans model). This situation is different from that of other canonical Reps, in which two N-terminal DNA-binding domains from the same dimeric unit form a dimer upon DNA binding (cis model). On the basis of these observations, we propose a noncanonical model for the reversible inactivation of a Rep by an Ant.
PubMed: 27099293
DOI: 10.1073/pnas.1602618113
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.98 Å)
Structure validation

226707

數據於2024-10-30公開中

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