3ep2: Difference between revisions

Revision as of 14:45, 17 December 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:3ep2.jpg

3ep2, resolution 9.00Å ()

Related:

2avy, 2aw4, 1qza, 1ob2, 3eq3, 3eq4

Structural annotation:
Resources:	InterPro : Ipr020785, Ipr020784, Ipr020783, Ipr006519, Ipr000911, Ipr012340, Ipr016027, Ipr006032, Ipr005679, Ipr004161, Ipr004160, Ipr000795, Ipr004541, Ipr005225, Ipr009001, Ipr009000 Pfam : PF03946, PF00298, PF00164

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EMModel of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM

Publication Abstract from PubMed

The accuracy of ribosomal translation is achieved by an initial selection and a proofreading step, mediated by EF-Tu, which forms a ternary complex with aminoacyl(aa)-tRNA. To study the binding modes of different aa-tRNAs, we compared cryo-EM maps of the kirromycin-stalled ribosome bound with ternary complexes containing Phe-tRNA(Phe), Trp-tRNA(Trp), or Leu-tRNA(LeuI). The three maps suggest a common binding manner of cognate aa-tRNAs in their specific binding with both the ribosome and EF-Tu. All three aa-tRNAs have the same 'loaded spring' conformation with a kink and twist between the D-stem and anticodon stem. The three complexes are similarly integrated in an interaction network, extending from the anticodon loop through h44 and protein S12 to the EF-Tu-binding CCA end of aa-tRNA, proposed to signal cognate codon-anticodon interaction to the GTPase centre and tune the accuracy of aa-tRNA selection.

Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM., Li W, Agirrezabala X, Lei J, Bouakaz L, Brunelle JL, Ortiz-Meoz RF, Green R, Sanyal S, Ehrenberg M, Frank J, EMBO J. 2008 Dec 17;27(24):3322-31. Epub 2008 Nov 20. PMID:19020518

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this StructureAbout this Structure

3EP2 is a 9 chains structure of sequences from Escherichia coli k12. Full crystallographic information is available from OCA.

ReferenceReference

Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM., Li W, Agirrezabala X, Lei J, Bouakaz L, Brunelle JL, Ortiz-Meoz RF, Green R, Sanyal S, Ehrenberg M, Frank J, EMBO J. 2008 Nov 20. PMID:19020518

Page seeded by OCA on Wed Dec 17 13:45:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{Seed}}
+[[Image:3ep2.jpg|left|200px]]
-The entry 3ep2 is ON HOLD  until Paper Publication
+<!--
+The line below this paragraph, containing "STRUCTURE_3ep2", creates the "Structure Box" on the page.
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+or leave the SCENE parameter empty for the default display.
+-->
+{{STRUCTURE_3ep2|  PDB=3ep2  |  SCENE=  }}
-Authors: Frank, J., Li, W., Agirrezabala, X.
+===Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM===
-Description: Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 22 10:17:21 2008''
+<!--
+The line below this paragraph, {{ABSTRACT_PUBMED_19020518}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 19020518 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_19020518}}
+==About this Structure==
+EP2 is a 9 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EP2 OCA].
+==Reference==
+Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM., Li W, Agirrezabala X, Lei J, Bouakaz L, Brunelle JL, Ortiz-Meoz RF, Green R, Sanyal S, Ehrenberg M, Frank J, EMBO J. 2008 Nov 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19020518 19020518]
+[[Category: Escherichia coli k12]]
+[[Category: Agirrezabala, X.]]
+[[Category: Frank, J.]]
+[[Category: Li, W.]]
+[[Category: A/t-trna]]
+[[Category: Acetylation]]
+[[Category: Antibiotic resistance]]
+[[Category: Automated data collection]]
+[[Category: Cytoplasm]]
+[[Category: Elongation factor]]
+[[Category: Gtp-binding]]
+[[Category: Membrane]]
+[[Category: Methylation]]
+[[Category: Nucleotide-binding]]
+[[Category: Phosphoprotein]]
+[[Category: Protein biosynthesis]]
+[[Category: Protein translation]]
+[[Category: Ribonucleoprotein]]
+[[Category: Ribosomal protein]]
+[[Category: Ribosomal protein/rna complex]]
+[[Category: Rna-binding]]
+[[Category: Rrna-binding]]
+[[Category: Ternary complex]]
+[[Category: Trna-binding]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 17 13:45:23 2008''