1yj9
From Proteopedia
(New page: 200px<br /><applet load="1yj9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yj9, resolution 2.80Å" /> '''Crystal Structure Of...) |
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| - | [[Image:1yj9.gif|left|200px]]<br /><applet load="1yj9" size=" | + | [[Image:1yj9.gif|left|200px]]<br /><applet load="1yj9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yj9, resolution 2.80Å" /> | caption="1yj9, resolution 2.80Å" /> | ||
'''Crystal Structure Of The Mutant 50S Ribosomal Subunit Of Haloarcula Marismortui Containing a three residue deletion in L22'''<br /> | '''Crystal Structure Of The Mutant 50S Ribosomal Subunit Of Haloarcula Marismortui Containing a three residue deletion in L22'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Crystal structures of H. marismortui large ribosomal subunits containing | + | Crystal structures of H. marismortui large ribosomal subunits containing the mutation G2099A (A2058 in E. coli) with erythromycin, azithromycin, clindamycin, virginiamycin S, and telithromycin bound explain why eubacterial ribosomes containing the mutation A2058G are resistant to them. Azithromycin binds almost identically to both G2099A and wild-type subunits, but the erythromycin affinity increases by more than 10(4)-fold, implying that desolvation of the N2 of G2099 accounts for the low wild-type affinity for macrolides. All macrolides bind similarly to the H. marismortui subunit, but their binding differs significantly from what has been reported in the D. radioidurans subunit. The synergy in the binding of streptogramins A and B appears to result from a reorientation of the base of A2103 (A2062, E. coli) that stacks between them. The structure of large subunit containing a three residue deletion mutant of L22 shows a change in the L22 structure and exit tunnel shape that illuminates its macrolide resistance phenotype. |
==About this Structure== | ==About this Structure== | ||
| - | 1YJ9 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 MG, K, NA, CD and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YJ9 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=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=1YJ9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Blaha, G.]] | [[Category: Blaha, G.]] | ||
| - | [[Category: Moore, P | + | [[Category: Moore, P B.]] |
| - | [[Category: Steitz, T | + | [[Category: Steitz, T A.]] |
[[Category: Tu, D.]] | [[Category: Tu, D.]] | ||
[[Category: CD]] | [[Category: CD]] | ||
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[[Category: mutated 50s subunits]] | [[Category: mutated 50s subunits]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:55 2008'' |
Revision as of 14:05, 21 February 2008
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Crystal Structure Of The Mutant 50S Ribosomal Subunit Of Haloarcula Marismortui Containing a three residue deletion in L22
Overview
Crystal structures of H. marismortui large ribosomal subunits containing the mutation G2099A (A2058 in E. coli) with erythromycin, azithromycin, clindamycin, virginiamycin S, and telithromycin bound explain why eubacterial ribosomes containing the mutation A2058G are resistant to them. Azithromycin binds almost identically to both G2099A and wild-type subunits, but the erythromycin affinity increases by more than 10(4)-fold, implying that desolvation of the N2 of G2099 accounts for the low wild-type affinity for macrolides. All macrolides bind similarly to the H. marismortui subunit, but their binding differs significantly from what has been reported in the D. radioidurans subunit. The synergy in the binding of streptogramins A and B appears to result from a reorientation of the base of A2103 (A2062, E. coli) that stacks between them. The structure of large subunit containing a three residue deletion mutant of L22 shows a change in the L22 structure and exit tunnel shape that illuminates its macrolide resistance phenotype.
About this Structure
1YJ9 is a Protein complex structure of sequences from Haloarcula marismortui with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance., Tu D, Blaha G, Moore PB, Steitz TA, Cell. 2005 Apr 22;121(2):257-70. PMID:15851032
Page seeded by OCA on Thu Feb 21 16:05:55 2008
Categories: Haloarcula marismortui | Protein complex | Blaha, G. | Moore, P B. | Steitz, T A. | Tu, D. | CD | CL | K | MG | NA | Deletion mutation | L22 | Mutated 50s subunits
