1bcx: Difference between revisions
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'''MUTATIONAL AND CRYSTALLOGRAPHIC ANALYSES OF THE ACTIVE SITE RESIDUES OF THE BACILLUS CIRCULANS XYLANASE''' | {{Structure | ||
|PDB= 1bcx |SIZE=350|CAPTION= <scene name='initialview01'>1bcx</scene>, resolution 1.81Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] | |||
|GENE= | |||
}} | |||
'''MUTATIONAL AND CRYSTALLOGRAPHIC ANALYSES OF THE ACTIVE SITE RESIDUES OF THE BACILLUS CIRCULANS XYLANASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BCX is a [ | 1BCX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BCX OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8019418 8019418] | ||
[[Category: Bacillus circulans]] | [[Category: Bacillus circulans]] | ||
[[Category: Endo-1,4-beta-xylanase]] | [[Category: Endo-1,4-beta-xylanase]] | ||
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[[Category: hydrolase(xylan degradation)]] | [[Category: hydrolase(xylan degradation)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:09:19 2008'' | ||
Revision as of 08:09, 20 March 2008
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| 1bcx, resolution 1.81Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Activity: | Endo-1,4-beta-xylanase, with EC number 3.2.1.8 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
MUTATIONAL AND CRYSTALLOGRAPHIC ANALYSES OF THE ACTIVE SITE RESIDUES OF THE BACILLUS CIRCULANS XYLANASE
Overview
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.
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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