2f4t: Difference between revisions

Revision as of 18:17, 21 February 2008

Asite RNA + designer antibiotic

OverviewOverview

The X-ray crystal structures for the complexes of three designer antibiotics, compounds 1, 2, and 3, bound to two models for the ribosomal aminoacyl-tRNA site (A site) at 2.5-3.0 Angstroms resolution and that of neamine at 2.8 Angstroms resolution are described. Furthermore, the complex of antibiotic 1 bound to the A site in the entire 30S ribosomal subunit of Thermus thermophilus is reported at 3.8 Angstroms resolution. Molecular dynamics simulations revealed that the designer compounds provide additional stability to bases A1492 and A1493 in their extrahelical forms. Snapshots from the simulations were used for free energy calculations, which revealed that van der Waals and hydrophobic effects were the driving forces behind the binding of designer antibiotic 3 when compared to the parental neamine.

About this StructureAbout this Structure

2F4T is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Interactions of designer antibiotics and the bacterial ribosomal aminoacyl-tRNA site., Murray JB, Meroueh SO, Russell RJ, Lentzen G, Haddad J, Mobashery S, Chem Biol. 2006 Feb;13(2):129-38. PMID:16492561

Page seeded by OCA on Thu Feb 21 17:17:40 2008

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OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-The X-ray crystal structures for the complexes of three designer, antibiotics, compounds 1, 2, and 3, bound to two models for the ribosomal, aminoacyl-tRNA site (A site) at 2.5-3.0 Angstroms resolution and that of, neamine at 2.8 Angstroms resolution are described. Furthermore, the, complex of antibiotic 1 bound to the A site in the entire 30S ribosomal, subunit of Thermus thermophilus is reported at 3.8 Angstroms resolution., Molecular dynamics simulations revealed that the designer compounds, provide additional stability to bases A1492 and A1493 in their, extrahelical forms. Snapshots from the simulations were used for free, energy calculations, which revealed that van der Waals and hydrophobic, effects were the driving forces behind the binding of designer antibiotic, 3 when compared to the parental neamine.
+The X-ray crystal structures for the complexes of three designer antibiotics, compounds 1, 2, and 3, bound to two models for the ribosomal aminoacyl-tRNA site (A site) at 2.5-3.0 Angstroms resolution and that of neamine at 2.8 Angstroms resolution are described. Furthermore, the complex of antibiotic 1 bound to the A site in the entire 30S ribosomal subunit of Thermus thermophilus is reported at 3.8 Angstroms resolution. Molecular dynamics simulations revealed that the designer compounds provide additional stability to bases A1492 and A1493 in their extrahelical forms. Snapshots from the simulations were used for free energy calculations, which revealed that van der Waals and hydrophobic effects were the driving forces behind the binding of designer antibiotic 3 when compared to the parental neamine.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Haddad, J.]]
 [[Category: Lentzen, G.]]
-[[Category: Meroueh, S.O.]]
+[[Category: Meroueh, S O.]]
 [[Category: Mobashery, S.]]
-[[Category: Murray, J.B.]]
+[[Category: Murray, J B.]]
-[[Category: Russell, R.J.]]
+[[Category: Russell, R J.]]
 [[Category: AB9]]
 [[Category: asite rna]]
 [[Category: designer antibiotic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:27:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:40 2008''