English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Topology of the polypeptide chain in the complex of agglutinin from castor bean seeds with β-D-galactose in the crystalline state

Konareva, N. V., Gabdulkhakov, A. G., Eschenburg, S., Stoeva, S., Popov, A. N., Krauspenhaar, R., et al. (2001). Topology of the polypeptide chain in the complex of agglutinin from castor bean seeds with β-D-galactose in the crystalline state. Crystallography Reports, 46(5), 792-800. doi:10.1134/1.1405866.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Topology of the polypeptide chain in the complex of agglutinin from castor bean seeds with β-D-galactose in the crystalline state

Files

show Files
hide Files
:
CrystallRep_46_2001_792.pdf (Any fulltext), 567KB
 
File Permalink:
-
Name:
CrystallRep_46_2001_792.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
http://dx.doi.org/10.1134/1.1405866 (Any fulltext)
Description:
-
Description:
-

Creators

show
hide
 Creators:
Konareva, N. V., Author
Gabdulkhakov, A. G., Author
Eschenburg, Susanne1, Author              
Stoeva, Stanka, Author
Popov, A. N., Author
Krauspenhaar, R., Author
Andrianova, M. E., Author
Savochkina, Y., Author
Agapov, I. I., Author
Tonevitskiframe, A. G., Author
Kornev, A. N., Author
Kornilov, V. V., Author
Zaitsev, V. N., Author
Voelter, Wolfgang J., Author
Betzel, Christian, Author
Nikonow, S. V., Author
Vainshtein, B. K., Author
Mikhailov, Alexander S., Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: The three-dimensional structure of the complex of agglutinin from Ricinus communis with β-D-galactose was established and refined at 2.5 Å resolution by X-ray structure analysis. Biocrystals were obtained using dialysis through a semipermeable membrane. X-ray intensity data (R merge = 4.6%) were collected from one crystal at 100 K using synchrotron radiation at the DESY outstation [European Molecular Biology Laboratory (EMBL), Hamburg, Germany]. The initial phases were calculated by the molecular replacement method. The atoms of both protein and sugar molecules were localized. Unlike ricin, the ricinlike heterodimer RcA contains only one galactose-binding center in the region of the Asn46-Gly25-Trp37-Lys40 site in the first domain of the B subunit, whereas the second galactose-binding site of the B subunit is lost. One functionally important water molecule, which is bound to the residues Tyr123-Glu176-Arg179-Glu207, was revealed in the region of the active center in the A subunit.

Details

show
hide
Language(s): eng - English
 Dates: 2001-04-252001-09-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666209
DOI: 10.1134/1.1405866
URI: http://www.springerlink.com/content/nq65285747l06105/
Other: 4958
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Crystallography Reports
  Other : Crystallogr. Rep.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: College Park, Md. : Published by MAIK Nauka/Interperiodika :
Pages: - Volume / Issue: 46 (5) Sequence Number: - Start / End Page: 792 - 800 Identifier: ISSN: 1063-7745
CoNE: https://pure.mpg.de/cone/journals/resource/954925599649