Polygalacturonase

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	== Structural highlights ==		== Structural highlights ==
-	This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.	+	The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity.
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	== References ==		== References ==
	<references/>		<references/>

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Revision as of 18:36, 12 July 2017

spinqualitylabelsall models PDB ID 1czf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Polygalacturonases (PGs) catalyze the enzymatic depolymerization of pectins – polysaccharides that comprise the plant cell wall. Polymer disassembly of substrates by exo- and endo- PGs is carried out via a hydrolytic mechanism. Degradation of pectins in plant cell walls contributes to ripening of fruits, such as tomatoes and melons (Polygalacturonases: many genes in search of a function).

Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights 5 References

Function

PGs cleave α-(1-4) – glycosidic bonds between consecutive galacturonic acid residues.

Disease

Relevance

Structural highlights

The secondary structure of PGs is comprised of a ten turn right handed beta helix domain along with two loop regions that together form the substrate-binding cleft, which appears to have a tunnel-like shape. The active site of PGs is found between the two looped regions of the protein. Located within the looped regions are two conserved aspartate residues that are predicted to participate in catalytic activity.

</StructureSection>

References