English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-TU, from Escherichia coli

Kabsch, W., Gast, W. H., Schulz, G. E., & Lebermann, R. (1977). Low resolution structure of partially trypsin-degraded polypeptide elongation factor, EF-TU, from Escherichia coli. Journal of Molecular Biology (London), 117(4), 999-1012. doi:10.1016/S0022-2836(77)80009-0.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-B11C-E Version Permalink: http://hdl.handle.net/21.11116/0000-0001-2BF2-E
Genre: Journal Article

Files

show Files
hide Files
:
JMolBiol_117_1977_999.pdf (Any fulltext), 3MB
 
File Permalink:
-
Name:
JMolBiol_117_1977_999.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Kabsch, Wolfgang1, 2, Author              
Gast, W. H., Author
Schulz, Georg E.1, Author              
Lebermann, Reuben, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: -
 Abstract: The low resolution structure of a trypsin-modified form of elongation factor EF-Tu from Escherichia coli has been determined by X-ray crystallographic methods. The crystals belong to space group P212121 with two molecules in the asymmetric unit. The phase determination was based on three isomorphous heavy-atom derivatives. The quality of the resulting electron density map at 6 Å was sufficient to identify the molecules. The two molecules in the asymmetric unit are related by a non-crystallographic 2-fold rotation. A molecular model was derived by averaging the electron density of the two molecules at equivalent points. Its overall dimensions are 75 Å × 50 Å × 35 Å. The molecule consists of a compact globular head of dimensions 45 Å × 40 Å × 40 Å and a curled tail of diameter 25 Å and length 55 Å. There is a second connection between head and tail, probably an α-helix, such that the molecule forms a ring. The large groove in the centre could accommodate a RNA double helix. The head has a high α-helical content whereas the tail seems to be helix-free. A molecular weight of 43,000 was derived from the electron density map indicating that no major part of the molecule is missing. Possible interactions between EF-Tu and transfer RNA are discussed.

Details

show
hide
Language(s): eng - English
 Dates: 1977-07-281977-09-202005-05-021977-12-25
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Academic Press
Pages: - Volume / Issue: 117 (4) Sequence Number: - Start / End Page: 999 - 1012 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042