1dq6: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1dq6.jpg|left|200px]]
{{Seed}}
[[Image:1dq6.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dq6|  PDB=1dq6  |  SCENE=  }}  
{{STRUCTURE_1dq6|  PDB=1dq6  |  SCENE=  }}  


'''Manganese;Manganese concanavalin A at pH 7.0'''
===Manganese;Manganese concanavalin A at pH 7.0===




==Overview==
<!--
The reversible binding of manganese and calcium to concanavalin A determines the carbohydrate binding of the lectin by inducing large conformational changes. These changes are governed by the isomerization of a non-proline peptide bond, Ala-207-Asp-208, positioned in a beta-strand in between the calcium binding site S2 and the carbohydrate specificity-determining loop. The replacement of calcium by manganese allowed us to investigate the structures of the carbohydrate binding, locked state and the inactive, unlocked state of concanavalin A, both with and without metal ions bound. Crystals of unlocked metal-free concanavalin A convert to the locked form with the binding of two Mn(2+) ions. Removal of these ions from the crystals traps metal-free concanavalin A in its locked state, a minority species in solution. The ligation of a metal ion in S2 to unlocked concanavalin A causes bending of the beta-strand foregoing the S2 ligand residues Asp-10 and Tyr-12. This bending disrupts conventional beta-sheet hydrogen bonding and forces the Thr-11 side chain against the Ala-207-Asp-208 peptide bond. The steric strain exerted by Thr-11 is presumed to drive the trans-to-cis isomerization. Upon isomerization, Asp-208 flips into its carbohydrate binding position, and the conformation of the carbohydrate specificity determining loop changes dramatically.
The line below this paragraph, {{ABSTRACT_PUBMED_10748006}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10748006 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10748006}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Manganese]]
[[Category: Manganese]]
[[Category: Metal binding]]
[[Category: Metal binding]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:08:39 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:27:05 2008''

Revision as of 20:27, 30 June 2008

File:1dq6.png

Template:STRUCTURE 1dq6

Manganese;Manganese concanavalin A at pH 7.0

Template:ABSTRACT PUBMED 10748006

About this Structure

1DQ6 is a Single protein structure of sequence from Canavalia ensiformis. Full crystallographic information is available from OCA.

Reference

The structural features of concanavalin A governing non-proline peptide isomerization., Bouckaert J, Dewallef Y, Poortmans F, Wyns L, Loris R, J Biol Chem. 2000 Jun 30;275(26):19778-87. PMID:10748006

Page seeded by OCA on Mon Jun 30 23:27:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1dq6&oldid=588605"