1h49
From Proteopedia
(Difference between revisions)
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[[Image:1h49.png|left|200px]] | [[Image:1h49.png|left|200px]] | ||
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===CRYSTAL STRUCTURE OF THE INACTIVE DOUBLE MUTANT OF THE MAIZE BETA-GLUCOSIDASE ZMGLU1-E191D-F198V IN COMPLEX WITH DIMBOA-GLUCOSIDE=== | ===CRYSTAL STRUCTURE OF THE INACTIVE DOUBLE MUTANT OF THE MAIZE BETA-GLUCOSIDASE ZMGLU1-E191D-F198V IN COMPLEX WITH DIMBOA-GLUCOSIDE=== | ||
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+ | <!-- | ||
+ | The line below this paragraph, {{ABSTRACT_PUBMED_12684498}}, adds the Publication Abstract to the page | ||
+ | (as it appears on PubMed at http://www.pubmed.gov), where 12684498 is the PubMed ID number. | ||
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+ | {{ABSTRACT_PUBMED_12684498}} | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[1h49]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H49 OCA]. | |
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+ | ==Reference== | ||
+ | <ref group="xtra">PMID:12684498</ref><ref group="xtra">PMID:11106394</ref><references group="xtra"/> | ||
[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Zea mays]] | [[Category: Zea mays]] | ||
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[[Category: Family 1]] | [[Category: Family 1]] | ||
[[Category: Glycoside hydrolase]] | [[Category: Glycoside hydrolase]] | ||
+ | [[Category: Hydrolase]] | ||
[[Category: Inactive mutant e191d]] | [[Category: Inactive mutant e191d]] | ||
[[Category: Retention of the anomeric configuration]] | [[Category: Retention of the anomeric configuration]] | ||
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- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 22 14:51:21 2010'' |
Revision as of 00:42, 15 March 2011
CRYSTAL STRUCTURE OF THE INACTIVE DOUBLE MUTANT OF THE MAIZE BETA-GLUCOSIDASE ZMGLU1-E191D-F198V IN COMPLEX WITH DIMBOA-GLUCOSIDE
Template:ABSTRACT PUBMED 12684498
About this Structure
1h49 is a 2 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA.
Reference
- Verdoucq L, Czjzek M, Moriniere J, Bevan DR, Esen A. Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases. J Biol Chem. 2003 Jul 4;278(27):25055-62. Epub 2003 Apr 8. PMID:12684498 doi:10.1074/jbc.M301978200
- 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