1e4l: Difference between revisions
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[[Image:1e4l.png|left|200px]] | [[Image:1e4l.png|left|200px]] | ||
{{STRUCTURE_1e4l| PDB=1e4l | SCENE= }} | {{STRUCTURE_1e4l| PDB=1e4l | SCENE= }} | ||
===CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZM GLU191ASP=== | ===CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZM GLU191ASP=== | ||
{{ABSTRACT_PUBMED_11106394}} | {{ABSTRACT_PUBMED_11106394}} | ||
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==See Also== | ==See Also== | ||
*[[Beta-glucosidase]] | *[[Beta-glucosidase|Beta-glucosidase]] | ||
==Reference== | ==Reference== | ||
Revision as of 03:53, 27 July 2012
CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZM GLU191ASP
Template:ABSTRACT PUBMED 11106394
About this Structure
1e4l is a 2 chain structure of Beta-glucosidase with sequence from Zea mays. Full crystallographic information is available from OCA.
See Also
Reference
- Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A. The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes. Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13555-60. PMID:11106394 doi:10.1073/pnas.97.25.13555
- Cicek M, Esen A. Expression of soluble and catalytically active plant (monocot) beta-glucosidases in E. coli. Biotechnol Bioeng. 1999 May 20;63(4):392-400. PMID:10099619