3b6a
From Proteopedia
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'''Crystal structure of the Streptomyces coelicolor TetR family protein ActR in complex with actinorhodin''' | '''Crystal structure of the Streptomyces coelicolor TetR family protein ActR in complex with actinorhodin''' | ||
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[[Category: Junop, M S.]] | [[Category: Junop, M S.]] | ||
[[Category: Willems, A R.]] | [[Category: Willems, A R.]] | ||
| - | [[Category: | + | [[Category: Actinorhodin]] |
| - | [[Category: | + | [[Category: Dna-binding protein]] |
| - | [[Category: | + | [[Category: Ligand]] |
| - | [[Category: | + | [[Category: Tetr family]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | [[Category: | + | [[Category: Transcriptional repressor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:25:58 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:25, 4 May 2008
Crystal structure of the Streptomyces coelicolor TetR family protein ActR in complex with actinorhodin
Overview
Actinorhodin, an antibiotic produced by Streptomyces coelicolor, is exported from the cell by the ActA efflux pump. actA is divergently transcribed from actR, which encodes a TetR-like transcriptional repressor. We showed previously that ActR represses transcription by binding to an operator from the actA/actR intergenic region. Importantly, actinorhodin itself or various actinorhodin biosynthetic intermediates can cause ActR to dissociate from its operator, leading to derepression. This suggests that ActR may mediate timely self-resistance to an endogenously produced antibiotic by responding to one of its biosynthetic precursors. Here, we report the structural basis for this precursor-mediated derepression with crystal structures of homodimeric ActR by itself and in complex with either actinorhodin or the actinorhodin biosynthetic intermediate (S)-DNPA [4-dihydro-9-hydroxy-1-methyl-10-oxo-3-H-naphtho-[2,3-c]-pyran-3-(S)-aceti c acid]. The ligand-binding tunnel in each ActR monomer has a striking hydrophilic/hydrophobic/hydrophilic arrangement of surface residues that accommodate either one hexacyclic actinorhodin molecule or two back-to-back tricyclic (S)-DNPA molecules. Moreover, our work also reveals the strongest structural evidence to date that TetR-mediated antibiotic resistance may have been acquired from an antibiotic-producer organism.
About this Structure
3B6A is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.
Reference
Crystal structures of the Streptomyces coelicolor TetR-like protein ActR alone and in complex with actinorhodin or the actinorhodin biosynthetic precursor (S)-DNPA., Willems AR, Tahlan K, Taguchi T, Zhang K, Lee ZZ, Ichinose K, Junop MS, Nodwell JR, J Mol Biol. 2008 Mar 7;376(5):1377-87. Epub 2008 Jan 4. PMID:18207163 Page seeded by OCA on Sun May 4 20:25:58 2008
