1e55: Difference between revisions
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[[Image:1e55.gif|left|200px]] | [[Image:1e55.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE COMPETITIVE INHIBITOR DHURRIN''' | '''CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE COMPETITIVE INHIBITOR DHURRIN''' | ||
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==About this Structure== | ==About this Structure== | ||
1E55 is a [[Single protein]] structure | 1E55 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E55 OCA]. | ||
==Reference== | ==Reference== | ||
The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes., Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13555-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106394 11106394] | The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes., Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13555-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106394 11106394] | ||
[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Henrissat, B.]] | [[Category: Henrissat, B.]] | ||
[[Category: Zamboni, V.]] | [[Category: Zamboni, V.]] | ||
[[Category: | [[Category: Beta-glucosidase]] | ||
[[Category: | [[Category: Complex with dhurrin]] | ||
[[Category: | [[Category: Family 1]] | ||
[[Category: | [[Category: Glycoside hydrolase]] | ||
[[Category: | [[Category: Inactive mutant e191d]] | ||
[[Category: | [[Category: Retention of the anomeric configuration]] | ||
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