Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/18851
Share/Export:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Title

Structure of concanavalin A at pH 8: bound solvent and crystal contacts

AuthorsLópez-Jaramillo, F. J.; González-Ramírez, L. A.; Albert, Armando CSIC ORCID; Santoyo-González, F.; Vargas-Berenguel, A.; Otalora, Fermín
KeywordsConcanavalin A
Issue DateJun-2004
PublisherInternational Union of Crystallography
CitationActa Crystallographica Section D 60(6): 1048-1056 (2004)
AbstractConcanavalin A has been crystallized in the presence of the ligand (6-S-[beta]-D-galactopyranosyl-6-thio)-cyclomaltoheptaose. The crystals are isomorphous to those reported for ConA complexed with peptides at low resolution (3.00-2.75 Å). The structure was solved at 1.9 Å, with free R and R values of 0.201 and 0.184, respectively. As expected, no molecules of the ligand were bound to the protein. Soaking in the cryobuffer left its fingerprint as 25 molecules of glycerol in the bound solvent, most of them at specific positions. The fact that a glycerol molecule is located in the sugar-binding pocket of each of the four subunits in the asymmetric unit and another is located in two of the peptide-binding sites suggests a recognition phenomenon rather than a displacement of water molecules by glycerol. Crystal contact analysis shows that a relation exists between the residues that form hydrogen bonds to other asymmetric units and the space group: contact Asp58-Ser62 is a universal feature of ConA crystals, while Ser66-His121, Asn69-Asn118 and Tyr100-His205 contacts are general features of the C2221 crystal form.
Description9 pages, 3 figures, 4 tables.
Publisher version (URL)http://dx.doi.org/10.1107/S0907444904007000
URIhttp://hdl.handle.net/10261/18851
DOI10.1107/S0907444904007000
ISSN1067-0696
Appears in Collections:(IACT) Artículos

Files in This Item:
File Description SizeFormat
fulltext.pdf854,1 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work

SCOPUSTM   
Citations

8
checked on Jan 20, 2022

WEB OF SCIENCETM
Citations

8
checked on Jan 14, 2022

Page view(s)

464
checked on Jan 20, 2022

Download(s)

328
checked on Jan 20, 2022

Google ScholarTM

Check

Altmetric

Dimensions


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.