2bm1
From Proteopedia
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'''RIBOSOMAL ELONGATION FACTOR G (EF-G) FUSIDIC ACID RESISTANT MUTANT G16V''' | '''RIBOSOMAL ELONGATION FACTOR G (EF-G) FUSIDIC ACID RESISTANT MUTANT G16V''' | ||
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[[Category: Logan, D T.]] | [[Category: Logan, D T.]] | ||
[[Category: Singh, R.]] | [[Category: Singh, R.]] | ||
| - | [[Category: | + | [[Category: Elongation factor]] |
| - | [[Category: | + | [[Category: Gtp-binding]] |
| - | [[Category: | + | [[Category: Mutation gly16val]] |
| - | [[Category: | + | [[Category: Protein biosynthesis]] |
| - | [[Category: | + | [[Category: Switch ii]] |
| - | [[Category: | + | [[Category: Translation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:28:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:28, 3 May 2008
RIBOSOMAL ELONGATION FACTOR G (EF-G) FUSIDIC ACID RESISTANT MUTANT G16V
Overview
Fusidic acid (FA) is a steroid antibiotic commonly used against Gram positive bacterial infections. It inhibits protein synthesis by stalling elongation factor G (EF-G) on the ribosome after translocation. A significant number of the mutations conferring strong FA resistance have been mapped at the interfaces between domains G, III and V of EF-G. However, direct information on how such mutations affect the structure has hitherto not been available. Here we present the crystal structures of two mutants of Thermus thermophilus EF-G, G16V and T84A, which exhibit FA hypersensitivity and resistance in vitro, respectively. These mutants also have higher and lower affinity for GTP respectively than wild-type EF-G. The mutations cause significant conformational changes in the switch II loop that have opposite effects on the position of a key residue, Phe90, which undergoes large conformational changes. This correlates with the importance of Phe90 in FA sensitivity reported in previous studies. These structures substantiate the importance of the domain G/domain III/domain V interfaces as a key component of the FA binding site. The mutations also cause subtle changes in the environment of the "P-loop lysine", Lys25. This led us to examine the conformation of the equivalent residue in all structures of translational GTPases, which revealed that EF-G and eEF2 form a group separate from the others and suggested that the role of Lys25 may be different in the two groups.
About this Structure
2BM1 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structural insights into fusidic acid resistance and sensitivity in EF-G., Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT, J Mol Biol. 2005 May 13;348(4):939-49. PMID:15843024 Page seeded by OCA on Sat May 3 20:28:29 2008
