1czf: Difference between revisions

Revision as of 21:51, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1czf, resolution 1.68Å ()

Ligands:

,

Activity:

Polygalacturonase, with EC number 3.2.1.15

Structural annotation:
Resources:	CATH : 1Czfa00, 1Czfb00 InterPro : Ipr000743, Ipr011050, Ipr006626, Ipr012334 Pfam : PF00295 SCOP : d1czfa_, d1czfb_ UniProt : P26214

Functional annotation:
Cellular component:	cell wall
Biological process:	metabolic process cell wall organization and biogenesis carbohydrate metabolic process
Molecular function:	hydrolase activity, acting on glycosyl bonds polygalacturonase activity hydrolase activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

ENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGERENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGER

Template:ABSTRACT PUBMED 10521427

About this StructureAbout this Structure

1CZF is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

ReferenceReference

1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis., van Santen Y, Benen JA, Schroter KH, Kalk KH, Armand S, Visser J, Dijkstra BW, J Biol Chem. 1999 Oct 22;274(43):30474-80. PMID:10521427

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OCA

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-'''ENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGER'''
+===ENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGER===
-==Overview==
+<!--
-Polygalacturonases specifically hydrolyze polygalacturonate, a major constituent of plant cell wall pectin. To understand the catalytic mechanism and substrate and product specificity of these enzymes, we have solved the x-ray structure of endopolygalacturonase II of Aspergillus niger and we have carried out site-directed mutagenesis studies. The enzyme folds into a right-handed parallel beta-helix with 10 complete turns. The beta-helix is composed of four parallel beta-sheets, and has one very small alpha-helix near the N terminus, which shields the enzyme's hydrophobic core. Loop regions form a cleft on the exterior of the beta-helix. Site-directed mutagenesis of Asp(180), Asp(201), Asp(202), His(223), Arg(256), and Lys(258), which are located in this cleft, results in a severe reduction of activity, demonstrating that these residues are important for substrate binding and/or catalysis. The juxtaposition of the catalytic residues differs from that normally encountered in inverting glycosyl hydrolases. A comparison of the endopolygalacturonase II active site with that of the P22 tailspike rhamnosidase suggests that Asp(180) and Asp(202) activate the attacking nucleophilic water molecule, while Asp(201) protonates the glycosidic oxygen of the scissile bond.
+The line below this paragraph, {{ABSTRACT_PUBMED_10521427}}, adds the Publication Abstract to the page
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