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.


1cnv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cnv.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1cnv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cnv| PDB=1cnv | SCENE= }}
{{STRUCTURE_1cnv| PDB=1cnv | SCENE= }}
-
'''CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION'''
+
===CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION===
-
==Overview==
+
<!--
-
Seeds of Canavalia ensiformis (jack bean) contain besides large amounts of canavalin and concanavalin A, a protein with a molecular mass of 33,800 which has been named concanavalin B. Although concanavalin B shares about 40% sequence identity with plant chitinases belonging to glycosyl hydrolase family 18, no chitinase activity could be detected for this protein. To resolve this incongruity concanavalin B was crystallised and its three-dimensional structure determined at 1.65 A (1 A = 0.1 nm) resolution. The structure consists of a single domain with a (beta/alpha)8 topology. A 30 amino acid residue long loop occurs between the second beta-strand of the barrel and the second alpha-helix. This extended loop is unusual for the (beta/alpha)8 topology, but appears in a similar conformation in the structures of the seed protein narbonin and several chitinases as well. Two non-proline cis-peptide bonds are present in the structure of concanavalin B: Ser34-Phe, and Trp265-Asn. This structural feature is rarely observed in proteins, but could also be identified in the three-dimensional structures of family 18 chitinases and narbonin in coincident positions. In the chitinases the aromatic residues of the non-proline cis-peptides have been proposed to have a function in the binding of the substrate. The region in concanavalin B, where in chitinases the active site is located, shows two significant differences. First, the catalytic glutamic acid is a glutamine in concanavalin B. Second, although part of the substrate binding cleft of the chitinases is present in concanavalin B, it is much shorter. From this we conclude that concanavalin B and family 18 chitinases are closely related, but that concanavalin B has lost its enzymatic function. It still may act as a carbohydrate binding protein, however.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7490746}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7490746 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7490746}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Chitin binding protein]]
[[Category: Chitin binding protein]]
[[Category: Plant chitinase]]
[[Category: Plant chitinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:55:54 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:00:01 2008''

Revision as of 18:00, 30 June 2008

Image:1cnv.png

Template:STRUCTURE 1cnv

CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION

Template:ABSTRACT PUBMED 7490746

About this Structure

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

Reference

Crystal structure of concanavalin B at 1.65 A resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis., Hennig M, Jansonius JN, Terwisscha van Scheltinga AC, Dijkstra BW, Schlesier B, J Mol Biol. 1995 Nov 24;254(2):237-46. PMID:7490746

Page seeded by OCA on Mon Jun 30 21:00:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cnv"
Personal tools