2hhh

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[[Image:2hhh.gif|left|200px]]<br /><applet load="2hhh" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hhh.gif|left|200px]]
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caption="2hhh, resolution 3.35&Aring;" />
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'''Crystal structure of kasugamycin bound to the 30S ribosomal subunit'''<br />
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{{Structure
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|PDB= 2hhh |SIZE=350|CAPTION= <scene name='initialview01'>2hhh</scene>, resolution 3.35&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=KSG:(1S,2R,3S,4R,5S,6S)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXYL 2-AMINO-4-{[CARBOXY(IMINO)METHYL]AMINO}-2,3,4,6-TETRADEOXY-ALPHA-D-ARABINO-HEXOPYRANOSIDE'>KSG</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of kasugamycin bound to the 30S ribosomal subunit'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2HHH is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=KSG:'>KSG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HHH OCA].
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2HHH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HHH OCA].
==Reference==
==Reference==
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The antibiotic kasugamycin mimics mRNA nucleotides to destabilize tRNA binding and inhibit canonical translation initiation., Schluenzen F, Takemoto C, Wilson DN, Kaminishi T, Harms JM, Hanawa-Suetsugu K, Szaflarski W, Kawazoe M, Shirouzu M, Nierhaus KH, Yokoyama S, Fucini P, Nat Struct Mol Biol. 2006 Oct;13(10):871-8. Epub 2006 Sep 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16998488 16998488]
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The antibiotic kasugamycin mimics mRNA nucleotides to destabilize tRNA binding and inhibit canonical translation initiation., Schluenzen F, Takemoto C, Wilson DN, Kaminishi T, Harms JM, Hanawa-Suetsugu K, Szaflarski W, Kawazoe M, Shirouzu M, Nierhaus KH, Yokoyama S, Fucini P, Nat Struct Mol Biol. 2006 Oct;13(10):871-8. Epub 2006 Sep 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16998488 16998488]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Schluenzen, F.]]
[[Category: Schluenzen, F.]]
[[Category: KSG]]
[[Category: KSG]]
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[[Category: 30s]]
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[[Category: 30]]
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[[Category: antibiotics]]
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[[Category: antibiotic]]
[[Category: initiation]]
[[Category: initiation]]
[[Category: ribosome]]
[[Category: ribosome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:17:15 2008''

Revision as of 15:17, 20 March 2008

Image:2hhh.gif


PDB ID 2hhh

Drag the structure with the mouse to rotate
, resolution 3.35Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



Crystal structure of kasugamycin bound to the 30S ribosomal subunit


Overview

Kasugamycin (Ksg) specifically inhibits translation initiation of canonical but not of leaderless messenger RNAs. Ksg inhibition is thought to occur by direct competition with initiator transfer RNA. The 3.35-A structure of Ksg bound to the 30S ribosomal subunit presented here provides a structural description of two Ksg-binding sites as well as a basis for understanding Ksg resistance. Notably, neither binding position overlaps with P-site tRNA; instead, Ksg mimics codon nucleotides at the P and E sites by binding within the path of the mRNA. Coupled with biochemical experiments, our results suggest that Ksg indirectly inhibits P-site tRNA binding through perturbation of the mRNA-tRNA codon-anticodon interaction during 30S canonical initiation. In contrast, for 70S-type initiation on leaderless mRNA, the overlap between mRNA and Ksg is reduced and the binding of tRNA is further stabilized by the presence of the 50S subunit, minimizing Ksg efficacy.

About this Structure

2HHH is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

The antibiotic kasugamycin mimics mRNA nucleotides to destabilize tRNA binding and inhibit canonical translation initiation., Schluenzen F, Takemoto C, Wilson DN, Kaminishi T, Harms JM, Hanawa-Suetsugu K, Szaflarski W, Kawazoe M, Shirouzu M, Nierhaus KH, Yokoyama S, Fucini P, Nat Struct Mol Biol. 2006 Oct;13(10):871-8. Epub 2006 Sep 24. PMID:16998488

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