1ocq
From Proteopedia
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| - | [[Image:1ocq.jpg|left|200px]]<br /><applet load="1ocq" size=" | + | [[Image:1ocq.jpg|left|200px]]<br /><applet load="1ocq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ocq, resolution 1.08Å" /> | caption="1ocq, resolution 1.08Å" /> | ||
'''COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM RESOLUTION WITH CELLOBIO-DERIVED ISOFAGOMINE'''<br /> | '''COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM RESOLUTION WITH CELLOBIO-DERIVED ISOFAGOMINE'''<br /> | ||
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| + | ==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. | ||
==About this Structure== | ==About this Structure== | ||
| - | 1OCQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens] with BGC, SO4, IFM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Known structural/functional Site: <scene name='pdbsite=NUC:So4 Binding Site For Chain A'>NUC</scene>. Full crystallographic information is available from [http:// | + | 1OCQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens] with <scene name='pdbligand=BGC:'>BGC</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=IFM:'>IFM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Known structural/functional Site: <scene name='pdbsite=NUC:So4+Binding+Site+For+Chain+A'>NUC</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:56:13 2008'' |
Revision as of 07:56, 3 February 2008
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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.
About this Structure
1OCQ is a Single protein structure of sequence from Bacillus agaradhaerens with , , and as ligands. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Direct observation of the protonation state of an imino sugar glycosidase inhibitor upon binding., Varrot A, Tarling CA, Macdonald JM, Stick RV, Zechel DL, Withers SG, Davies GJ, J Am Chem Soc. 2003 Jun 25;125(25):7496-7. PMID:12812472
Page seeded by OCA on Sun Feb 3 09:56:13 2008
Categories: Bacillus agaradhaerens | Cellulase | Single protein | Davies, G.J. | Macdonald, J. | Stick, R.V. | Varrot, A. | Withers, S.G. | BGC | GOL | IFM | SO4 | Cellulose degradation | Endoglucanase | Glycosidase | Hydrolase
