1mac: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1mac.jpg|left|200px]]
{{Seed}}
[[Image:1mac.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mac|  PDB=1mac  |  SCENE=  }}  
{{STRUCTURE_1mac|  PDB=1mac  |  SCENE=  }}  


'''CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF BACILLUS MACERANS ENDO-1,3-1,4-BETA-GLUCANASE'''
===CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF BACILLUS MACERANS ENDO-1,3-1,4-BETA-GLUCANASE===




==Overview==
<!--  
In beta-glucans those beta-1,4 glycosidic bonds which are adjacent to beta-1,3 bonds are cleaved by endo-1,3-1,4-beta-glucanases (beta-glucanases). Here, the relationship between structure and activity of the beta-glucanase of Bacillus macerans is studied by x-ray crystallography and site-directed mutagenesis of active site residues. Crystal structure analysis at 2.3-A resolution reveals a jelly-roll protein structure with a deep active site channel harboring the amino acid residues Trp101, Glu103, Asp105, and Glu107 as in the hybrid Bacillus beta-glucanase H(A16-M) (Keitel, T., Simon, O., Borriss, R., and Heinemann, U. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 5287-5291). Different mutant proteins with substitutions in these residues are generated by site-directed mutagenesis, isolated, and characterized. Compared with the wild-type enzyme their activity is reduced to less than 1%. Several mutants with isosteric substitutions in Glu103 and Glu107 are completely inactive, suggesting a direct role of these residues in glycosyl bond hydrolysis. The kinetic properties of mutant beta-glucanases and the crystal structure of the wild-type enzyme are consistent with a mechanism where Glu103 and Glu107 are the catalytic amino acid residues responsible for cleavage of the beta-1,4 glycosidic bond within the substrate molecule.
The line below this paragraph, {{ABSTRACT_PUBMED_7852389}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7852389 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7852389}}


==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Hahn, M.]]
[[Category: Hahn, M.]]
[[Category: Heinemann, U.]]
[[Category: Heinemann, U.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:49:21 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:33:17 2008''