This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ob5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ob5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ob5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ob5| PDB=1ob5 | SCENE= }}
{{STRUCTURE_1ob5| PDB=1ob5 | SCENE= }}
-
'''T. AQUATICUS ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC ENACYLOXIN IIA, A GTP ANALOG, AND PHE-TRNA'''
+
===T. AQUATICUS ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC ENACYLOXIN IIA, A GTP ANALOG, AND PHE-TRNA===
-
==Overview==
+
<!--
-
Elongation factor (EF-) Tu.GTP is the carrier of aminoacyl-tRNA to the programmed ribosome. Enacyloxin IIa inhibits bacterial protein synthesis by hindering the release of EF-Tu.GDP from the ribosome. The crystal structure of the Escherichia coli EF-Tu.guanylyl iminodiphosphate (GDPNP).enacyloxin IIa complex at 2.3 A resolution presented here reveals the location of the antibiotic at the interface of domains 1 and 3. The binding site overlaps that of kirromycin, an antibiotic with a structure that is unrelated to enacyloxin IIa but that also inhibits EF-Tu.GDP release. As one of the major differences, the enacyloxin IIa tail borders a hydrophobic pocket that is occupied by the longer tail of kirromycin, explaining the higher binding affinity of the latter. EF-Tu.GDPNP.enacyloxin IIa shows a disordered effector region that in the Phe-tRNAPhe.EF-Tu (Thermus aquaticus).GDPNP.enacyloxin IIa complex, solved at 3.1 A resolution, is stabilized by the interaction with tRNA. This work clarifies the structural background of the action of enacyloxin IIa and compares its properties with those of kirromycin, opening new perspectives for structure-guided design of novel antibiotics.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16257965}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16257965 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16257965}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Transfer rna]]
[[Category: Transfer rna]]
[[Category: Translation elongation factor]]
[[Category: Translation elongation factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:37:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:40:28 2008''

Revision as of 16:40, 28 July 2008

Image:1ob5.png

Template:STRUCTURE 1ob5

T. AQUATICUS ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC ENACYLOXIN IIA, A GTP ANALOG, AND PHE-TRNA

Template:ABSTRACT PUBMED 16257965

About this Structure

1OB5 is a Protein complex structure of sequences from Thermus aquaticus. Full crystallographic information is available from OCA.

Reference

Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibiotics., Parmeggiani A, Krab IM, Watanabe T, Nielsen RC, Dahlberg C, Nyborg J, Nissen P, J Biol Chem. 2006 Feb 3;281(5):2893-900. Epub 2005 Oct 28. PMID:16257965

Page seeded by OCA on Mon Jul 28 19:40:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ob5"
Personal tools