1bcx

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{{STRUCTURE_1bcx| PDB=1bcx | SCENE= }}
{{STRUCTURE_1bcx| PDB=1bcx | SCENE= }}
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'''MUTATIONAL AND CRYSTALLOGRAPHIC ANALYSES OF THE ACTIVE SITE RESIDUES OF THE BACILLUS CIRCULANS XYLANASE'''
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===MUTATIONAL AND CRYSTALLOGRAPHIC ANALYSES OF THE ACTIVE SITE RESIDUES OF THE BACILLUS CIRCULANS XYLANASE===
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==Overview==
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Using site-directed mutagenesis we have investigated the catalytic residues in a xylanase from Bacillus circulans. Analysis of the mutants E78D and E172D indicated that mutations in these conserved residues do not grossly alter the structure of the enzyme and that these residues participate in the catalytic mechanism. We have now determined the crystal structure of an enzyme-substrate complex to 108 A resolution using a catalytically incompetent mutant (E172C). In addition to the catalytic residues, Glu 78 and Glu 172, we have identified 2 tyrosine residues, Tyr 69 and Tyr 80, which likely function in substrate binding, and an arginine residue, Arg 112, which plays an important role in the active site of this enzyme. On the basis of our work we would propose that Glu 78 is the nucleophile and that Glu 172 is the acid-base catalyst in the reaction.
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{{ABSTRACT_PUBMED_8019418}}
==About this Structure==
==About this Structure==
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[[Category: Campbell, R L.]]
[[Category: Campbell, R L.]]
[[Category: Wakarchuk, W W.]]
[[Category: Wakarchuk, W W.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:51:33 2008''

Revision as of 15:51, 30 June 2008

Image:1bcx.png

Template:STRUCTURE 1bcx

MUTATIONAL AND CRYSTALLOGRAPHIC ANALYSES OF THE ACTIVE SITE RESIDUES OF THE BACILLUS CIRCULANS XYLANASE

Template:ABSTRACT PUBMED 8019418

About this Structure

1BCX is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase., Wakarchuk WW, Campbell RL, Sung WL, Davoodi J, Yaguchi M, Protein Sci. 1994 Mar;3(3):467-75. PMID:8019418

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