2bm1
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2bm1 |SIZE=350|CAPTION= <scene name='initialview01'>2bm1</scene>, resolution 2.6Å | |PDB= 2bm1 |SIZE=350|CAPTION= <scene name='initialview01'>2bm1</scene>, resolution 2.6Å | ||
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bm1 OCA], [http://www.ebi.ac.uk/pdbsum/2bm1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bm1 RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Logan, D T.]] | [[Category: Logan, D T.]] | ||
[[Category: Singh, R.]] | [[Category: Singh, R.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: elongation factor]] | [[Category: elongation factor]] | ||
[[Category: gtp-binding]] | [[Category: gtp-binding]] | ||
| Line 36: | Line 37: | ||
[[Category: translation]] | [[Category: translation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:08:22 2008'' |
Revision as of 23:08, 30 March 2008
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 02:08:22 2008
