2d05

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[[Image:2d05.gif|left|200px]]
[[Image:2d05.gif|left|200px]]
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{{Structure
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|PDB= 2d05 |SIZE=350|CAPTION= <scene name='initialview01'>2d05</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_2d05", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitosanase Chitosanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.132 3.2.1.132] </span>
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{{STRUCTURE_2d05| PDB=2d05 | SCENE= }}
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|RELATEDENTRY=[[1qgi|1QGI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d05 OCA], [http://www.ebi.ac.uk/pdbsum/2d05 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d05 RCSB]</span>
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'''Chitosanase From Bacillus circulans mutant K218P'''
'''Chitosanase From Bacillus circulans mutant K218P'''
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[[Category: Yamaguchi, K.]]
[[Category: Yamaguchi, K.]]
[[Category: Yoshikawa, T.]]
[[Category: Yoshikawa, T.]]
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[[Category: chitosan degradation]]
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[[Category: Chitosan degradation]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:27:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:28:34 2008''
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Revision as of 20:27, 3 May 2008

Template:STRUCTURE 2d05

Chitosanase From Bacillus circulans mutant K218P


Overview

To identify the amino acids responsible for the substrate binding of chitosanase from Bacillus circulans MH-K1 (MH-K1 chitosanase), Tyr148 and Lys218 of the chitosanase were mutated to serine and proline, respectively, and the mutated chitosanases were characterized. The enzymatic activities of Y148S and K218P were found to be 12.5% and 0.16% of the wild type, respectively. When the (GlcN)3 binding ability to the chitosanase was evaluated by fluorescence spectroscopy and thermal unfolding experiments, the binding abilities of both mutant enzymes were markedly reduced as compared with the wild type enzyme. The affinity of the enzyme for the trisaccharide decreased by 1.0 kcal/mol of binding free energy for Y148S, and 3.7 kcal/mol for K218P. The crystal structure of K218P revealed that Pro218 forms a cis-peptide bond and that the state of the flexible loop containing the 218th residue is considerably affected by the mutation. Thus, we conclude that the flexible loop containing Lys218 plays an important role in substrate binding, and that the role of Tyr148 is less critical, but still important, due to a stacking interaction or hydrogen bond.

About this Structure

2D05 is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

Bacillus circulans MH-K1 chitosanase: amino acid residues responsible for substrate binding., Fukamizo T, Amano S, Yamaguchi K, Yoshikawa T, Katsumi T, Saito J, Suzuki M, Miki K, Nagata Y, Ando A, J Biochem. 2005 Nov;138(5):563-9. PMID:16272568 Page seeded by OCA on Sat May 3 23:27:16 2008

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