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Structure of soncanavalin A at 4 A resolution
Summary
Concanavalin A, a jack bean phytohemagglutinin, was analyzed using X-ray diffraction. Its molecular structure and potential saccharide binding site were revealed at 4 A resolution.
Area of Science:
- Biochemistry
- Structural Biology
- Crystallography
Background:
- Concanavalin A is a phytohemagglutinin from the jack bean.
- Understanding its structure is crucial for its biological functions.
Purpose of the Study:
- To determine the three-dimensional structure of Concanavalin A.
- To identify potential saccharide binding sites.
Main Methods:
- X-ray diffraction analysis of native Concanavalin A and heavy-metal derivatives.
- Structure refinement using least-squares methods to 4 A resolution.
Main Results:
- The crystal structure of Concanavalin A was determined at 4 A resolution.
- The asymmetric unit (27,000 mol wt) forms a "gumdrop" shape.
- Subunits form dimers, which then form tetrahedral tetramers.
- A depression on the molecular surface suggests a saccharide binding site.
- The polypeptide chain course was traced in many regions.
Conclusions:
- The study elucidated the quaternary structure of Concanavalin A.
- A potential saccharide binding site was identified based on structural features.