We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1w3a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1w3a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1w3a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1w3a| PDB=1w3a | SCENE= }}
{{STRUCTURE_1w3a| PDB=1w3a | SCENE= }}
-
'''THREE DIMENSIONAL STRUCTURE OF A NOVEL PORE-FORMING LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS'''
+
===THREE DIMENSIONAL STRUCTURE OF A NOVEL PORE-FORMING LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS===
-
==Overview==
+
<!--
-
LSL is a lectin produced by the parasitic mushroom Laetiporus sulphureus, which exhibits hemolytic and hemagglutinating activities. Here, we report the crystal structure of LSL refined to 2.6-A resolution determined by the single isomorphous replacement method with the anomalous scatter (SIRAS) signal of a platinum derivative. The structure reveals that LSL is hexameric, which was also shown by analytical ultracentrifugation. The monomeric protein (35 kDa) consists of two distinct modules: an N-terminal lectin module and a pore-forming module. The lectin module has a beta-trefoil scaffold that bears structural similarities to those present in toxins known to interact with galactose-related carbohydrates such as the hemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum, abrin, and ricin. On the other hand, the C-terminal pore-forming module (composed of domains 2 and 3) exhibits three-dimensional structural resemblances with domains 3 and 4 of the beta-pore-forming toxin aerolysin from the Gram-negative bacterium Aeromonas hydrophila, and domains 2 and 3 from the epsilon-toxin from Clostridium perfringens. This finding reveals the existence of common structural elements within the aerolysin-like family of toxins that could be directly involved in membrane-pore formation. The crystal structures of the complexes of LSL with lactose and N-acetyllactosamine reveal two dissacharide-binding sites per subunit and permits the identification of critical residues involved in sugar binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15687495}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15687495 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15687495}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Oligomer]]
[[Category: Oligomer]]
[[Category: Pore-forming toxin]]
[[Category: Pore-forming toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:05:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:07:24 2008''

Revision as of 11:07, 29 July 2008

Image:1w3a.png

Template:STRUCTURE 1w3a

THREE DIMENSIONAL STRUCTURE OF A NOVEL PORE-FORMING LECTIN FROM THE MUSHROOM LAETIPORUS SULPHUREUS

Template:ABSTRACT PUBMED 15687495

About this Structure

1W3A is a Single protein structure of sequence from Laetiporus sulphureus. Full crystallographic information is available from OCA.

Reference

Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars., Mancheno JM, Tateno H, Goldstein IJ, Martinez-Ripoll M, Hermoso JA, J Biol Chem. 2005 Apr 29;280(17):17251-9. Epub 2005 Feb 1. PMID:15687495

Page seeded by OCA on Tue Jul 29 14:07:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w3a"
Personal tools