3b6c

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[[Image:3b6c.jpg|left|200px]]<br /><applet load="3b6c" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:3b6c.jpg|left|200px]]
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caption="3b6c, resolution 2.30&Aring;" />
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'''Crystal structure of the Streptomyces coelicolor TetR family protein ActR in complex with (S)-DNPA'''<br />
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{{Structure
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|PDB= 3b6c |SIZE=350|CAPTION= <scene name='initialview01'>3b6c</scene>, resolution 2.30&Aring;
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|SITE= <scene name='pdbsite=AC1:Sdn+Binding+Site+For+Residue+A+301'>AC1</scene>, <scene name='pdbsite=AC2:Sdn+Binding+Site+For+Residue+A+302'>AC2</scene> and <scene name='pdbsite=AC3:Sdn+Binding+Site+For+Residue+B+303'>AC3</scene>
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|LIGAND= <scene name='pdbligand=SDN:'>SDN</scene>
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|ACTIVITY=
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|GENE= actII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 Streptomyces coelicolor])
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}}
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'''Crystal structure of the Streptomyces coelicolor TetR family protein ActR in complex with (S)-DNPA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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3B6C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=SDN:'>SDN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=AC1:Sdn+Binding+Site+For+Residue+A+301'>AC1</scene>, <scene name='pdbsite=AC2:Sdn+Binding+Site+For+Residue+A+302'>AC2</scene> and <scene name='pdbsite=AC3:Sdn+Binding+Site+For+Residue+B+303'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B6C OCA].
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3B6C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B6C OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18207163 18207163]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18207163 18207163]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
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[[Category: transcriptional repressor]]
[[Category: transcriptional repressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 5 13:26:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:56:29 2008''

Revision as of 16:56, 20 March 2008


PDB ID 3b6c

Drag the structure with the mouse to rotate
, resolution 2.30Å
Sites: , and
Ligands:
Gene: actII (Streptomyces coelicolor)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the Streptomyces coelicolor TetR family protein ActR in complex with (S)-DNPA


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

3B6C 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

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