1gic: Difference between revisions

Revision as of 05:20, 1 July 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:1gic.png

Template:STRUCTURE 1gic

CONCANAVALIN A COMPLEXED WITH METHYL ALPHA-D-GLUCOPYRANOSIDECONCANAVALIN A COMPLEXED WITH METHYL ALPHA-D-GLUCOPYRANOSIDE

Template:ABSTRACT PUBMED 15299735

About this StructureAbout this Structure

1GIC is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.

ReferenceReference

Structure solution of a cubic crystal of concanavalin A complexed with methyl alpha-D-glucopyranoside., Harrop SJ, Helliwell JR, Wan TC, Kalb AJ, Tong L, Yariv J, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):143-55. PMID:15299735

Page seeded by OCA on Tue Jul 1 05:20:25 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1gic.jpg|left|200px]]
+{{Seed}}
+[[Image:1gic.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1gic|  PDB=1gic  |  SCENE=  }}
-'''CONCANAVALIN A COMPLEXED WITH METHYL ALPHA-D-GLUCOPYRANOSIDE'''
+===CONCANAVALIN A COMPLEXED WITH METHYL ALPHA-D-GLUCOPYRANOSIDE===
-==Overview==
+<!--
-The solution of the cubic crystal form (a = 167.8 A) of concanavalin A complexed with the monosaccharide methyl alpha-D-glucopyranoside is described. The space group has been determined as I2(1)3 rather than I23. The use of cadmium to replace cobalt at the transition metal-ion binding site and to replace calcium at its binding site proved to be crucial to the successful solution of the crystal structure. The relatively small isomorphous signals of 21 e(-) for the replacement of cobalt and 28 e(-) for the replacement of calcium, yielded interpretable difference Patterson maps. The electron-density map calculated in space group I2(1)3 at 5.4 A resolution, based on phases derived from single- and double-substituted cadmium differences, revealed a classical concanavalin A tetramer of 222 point symmetry, as seen in all the known crystal structures of concanavalin A. Rigid-body refinement at 3.6 A using the refined coordinates of saccharide-free concanavalin A converged to an R factor of 27.4%. A molecular-replacement analysis, consistent with this crystal structure, and initial experiences in the incorrect space group I23 are described as these also prove to be instructive.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299735}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299735 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299735}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Lectin]]
 [[Category: Saccharide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:36:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 05:20:25 2008''