This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2enr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2enr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2enr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2enr| PDB=2enr | SCENE= }}
{{STRUCTURE_2enr| PDB=2enr | SCENE= }}
-
'''CO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH CADMIUM HAVING A CADMIUM ION BOUND IN BOTH THE S1 SITE AND THE S2 SITE'''
+
===CO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH CADMIUM HAVING A CADMIUM ION BOUND IN BOTH THE S1 SITE AND THE S2 SITE===
-
==Overview==
+
<!--
-
The crystal structures of cadmium/cadmium and zinc/calcium concanavalin A (con A) at pH 5.0 and pH 6.15, respectively, were determined. The structure of cadmium/cadmium con A confirms that the secondary Cd(2+)-binding site S3 is empty at pH 5. The metal-binding sites S1 and S2 are only very slightly affected by the substitution with cadmium. On the other hand, S1 and S2 and most of the protein surface of zinc/calcium con A at pH 6.15 differ from other fully metal-bound and carbohydrate-free structures. Most of these structural differences at the protein surface are a result of the interplay between metal binding, protonation and crystal packing. This interplay is expressed by relative rotations and translations of the con A units in alternative crystal packings and participation in space-group conversions inside crystals in situ. The particular crystal packing of zinc/calcium con A creates a novel zinc-binding site S4. The Zn(2+) ion in S4 ligates two aspartates from one tetramer and a histidine from a symmetry-related tetramer.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11092923}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11092923 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11092923}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Metal binding]]
[[Category: Metal binding]]
[[Category: Plant lectin]]
[[Category: Plant lectin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:51:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:40:33 2008''

Revision as of 03:40, 29 July 2008

Image:2enr.png

Template:STRUCTURE 2enr

CO-CRYSTALS OF DEMETALLIZED CONCANAVALIN A WITH CADMIUM HAVING A CADMIUM ION BOUND IN BOTH THE S1 SITE AND THE S2 SITE

Template:ABSTRACT PUBMED 11092923

About this Structure

2ENR is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.

Reference

Zinc/calcium- and cadmium/cadmium-substituted concanavalin A: interplay of metal binding, pH and molecular packing., Bouckaert J, Loris R, Wyns L, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1569-76. PMID:11092923

Page seeded by OCA on Tue Jul 29 06:40:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2enr"
Personal tools