1ocq: Difference between revisions

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[[Image:1ocq.~~jpg~~|left|200px]]

[[Image:1ocq.png|left|200px]]

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~~'''~~COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM RESOLUTION WITH CELLOBIO-DERIVED ISOFAGOMINE~~'''~~

===COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM RESOLUTION WITH CELLOBIO-DERIVED ISOFAGOMINE===

~~==Overview==~~

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~~Glycosidases are some of~~ the ~~most ubiquitous enzyme in nature. Their biological significance, coupled~~ to ~~their enormous catalytic prowess derived from tight binding of~~ the ~~transition state, is reflected in their importance~~ as ~~therapeutic targets~~. ~~Many glycosidase inhibitors are known~~. ~~Imino sugars are often potent inhibitors~~, ~~yet many facets of their mode of action, such as their degree, if any, of transition-state "mimicry" and their protonation state when bound to~~ the ~~target glycosidase remain unclear~~. ~~Atomic resolution analysis of the endoglucanase, Cel5A, in complex with a cellobio~~-derived isofagomine in conjunction with the pH dependence of Ki and kcat/KM reveals that this compound binds as a protonated sugar. Surprisingly, both the enzymatic nucleophile and the acid/base are unprotonated in the complex.

The line below this paragraph, {{ABSTRACT_PUBMED_12812472}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12812472 is the PubMed ID number.

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==About this Structure==

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[[Category: Glycosidase]]

[[Category: Hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 03~~:40:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:59:59 2008''

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-[[Image:1ocq.jpg|left|200px]]
+{{Seed}}
+[[Image:1ocq.png|left|200px]]
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 {{STRUCTURE_1ocq|  PDB=1ocq  |  SCENE=  }}
-'''COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM RESOLUTION WITH CELLOBIO-DERIVED ISOFAGOMINE'''
+===COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM RESOLUTION WITH CELLOBIO-DERIVED ISOFAGOMINE===
-==Overview==
+<!--
-Glycosidases are some of the most ubiquitous enzyme in nature. Their biological significance, coupled to their enormous catalytic prowess derived from tight binding of the transition state, is reflected in their importance as therapeutic targets. Many glycosidase inhibitors are known. Imino sugars are often potent inhibitors, yet many facets of their mode of action, such as their degree, if any, of transition-state "mimicry" and their protonation state when bound to the target glycosidase remain unclear. Atomic resolution analysis of the endoglucanase, Cel5A, in complex with a cellobio-derived isofagomine in conjunction with the pH dependence of Ki and kcat/KM reveals that this compound binds as a protonated sugar. Surprisingly, both the enzymatic nucleophile and the acid/base are unprotonated in the complex.
+The line below this paragraph, {{ABSTRACT_PUBMED_12812472}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12812472 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12812472}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Glycosidase]]
 [[Category: Hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:40:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:59:59 2008''