1kc8: Difference between revisions
New page: left|200px<br /><applet load="1kc8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kc8, resolution 3.01Å" /> '''Co-crystal Structure... |
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[[Image:1kc8.gif|left|200px]]<br /><applet load="1kc8" size=" | [[Image:1kc8.gif|left|200px]]<br /><applet load="1kc8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1kc8, resolution 3.01Å" /> | caption="1kc8, resolution 3.01Å" /> | ||
'''Co-crystal Structure of Blasticidin S Bound to the 50S Ribosomal Subunit'''<br /> | '''Co-crystal Structure of Blasticidin S Bound to the 50S Ribosomal Subunit'''<br /> | ||
==Overview== | ==Overview== | ||
Structures of anisomycin, chloramphenicol, sparsomycin, blasticidin S, and | Structures of anisomycin, chloramphenicol, sparsomycin, blasticidin S, and virginiamycin M bound to the large ribosomal subunit of Haloarcula marismortui have been determined at 3.0A resolution. Most of these antibiotics bind to sites that overlap those of either peptidyl-tRNA or aminoacyl-tRNA, consistent with their functioning as competitive inhibitors of peptide bond formation. Two hydrophobic crevices, one at the peptidyl transferase center and the other at the entrance to the peptide exit tunnel play roles in binding these antibiotics. Midway between these crevices, nucleotide A2103 of H.marismortui (2062 Escherichia coli) varies in its conformation and thereby contacts antibiotics bound at either crevice. The aromatic ring of anisomycin binds to the active-site hydrophobic crevice, as does the aromatic ring of puromycin, while the aromatic ring of chloramphenicol binds to the exit tunnel hydrophobic crevice. Sparsomycin contacts primarily a P-site bound substrate, but also extends into the active-site hydrophobic crevice. Virginiamycin M occupies portions of both the A and P-site, and induces a conformational change in the ribosome. Blasticidin S base-pairs with the P-loop and thereby mimics C74 and C75 of a P-site bound tRNA. | ||
==About this Structure== | ==About this Structure== | ||
1KC8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with BLS, MG, K, NA, CD and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1KC8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui] with <scene name='pdbligand=BLS:'>BLS</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KC8 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ban, N.]] | [[Category: Ban, N.]] | ||
[[Category: Hansen, J | [[Category: Hansen, J L.]] | ||
[[Category: Moore, P | [[Category: Moore, P B.]] | ||
[[Category: Nissen, P.]] | [[Category: Nissen, P.]] | ||
[[Category: Steitz, T | [[Category: Steitz, T A.]] | ||
[[Category: BLS]] | [[Category: BLS]] | ||
[[Category: CD]] | [[Category: CD]] | ||
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[[Category: p-site]] | [[Category: p-site]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:26 2008'' | ||
Revision as of 14:32, 21 February 2008
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Co-crystal Structure of Blasticidin S Bound to the 50S Ribosomal Subunit
OverviewOverview
Structures of anisomycin, chloramphenicol, sparsomycin, blasticidin S, and virginiamycin M bound to the large ribosomal subunit of Haloarcula marismortui have been determined at 3.0A resolution. Most of these antibiotics bind to sites that overlap those of either peptidyl-tRNA or aminoacyl-tRNA, consistent with their functioning as competitive inhibitors of peptide bond formation. Two hydrophobic crevices, one at the peptidyl transferase center and the other at the entrance to the peptide exit tunnel play roles in binding these antibiotics. Midway between these crevices, nucleotide A2103 of H.marismortui (2062 Escherichia coli) varies in its conformation and thereby contacts antibiotics bound at either crevice. The aromatic ring of anisomycin binds to the active-site hydrophobic crevice, as does the aromatic ring of puromycin, while the aromatic ring of chloramphenicol binds to the exit tunnel hydrophobic crevice. Sparsomycin contacts primarily a P-site bound substrate, but also extends into the active-site hydrophobic crevice. Virginiamycin M occupies portions of both the A and P-site, and induces a conformational change in the ribosome. Blasticidin S base-pairs with the P-loop and thereby mimics C74 and C75 of a P-site bound tRNA.
About this StructureAbout this Structure
1KC8 is a Protein complex structure of sequences from Haloarcula marismortui with , , , , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit., Hansen JL, Moore PB, Steitz TA, J Mol Biol. 2003 Jul 25;330(5):1061-75. PMID:12860128
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