1yhq: Difference between revisions

Revision as of 02:25, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1yhq.png

Template:STRUCTURE 1yhq

Crystal Structure Of Azithromycin Bound To The G2099A Mutant 50S Ribosomal Subunit Of Haloarcula MarismortuiCrystal Structure Of Azithromycin Bound To The G2099A Mutant 50S Ribosomal Subunit Of Haloarcula Marismortui

Template:ABSTRACT PUBMED 15851032

About this StructureAbout this Structure

1YHQ is a Protein complex structure of sequences from Haloarcula marismortui. Full crystallographic information is available from OCA.

ReferenceReference

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 Mon Jul 28 02:25:44 2008

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-'''Crystal Structure Of Azithromycin Bound To The G2099A Mutant 50S Ribosomal Subunit Of Haloarcula Marismortui'''
+===Crystal Structure Of Azithromycin Bound To The G2099A Mutant 50S Ribosomal Subunit Of Haloarcula Marismortui===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15851032}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15851032 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15851032}}
 ==About this Structure==
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 [[Category: Azithromycin]]
 [[Category: Mutated 50s subunit]]
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