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1ocq

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Revision as of 08:15, 22 July 2015

COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM RESOLUTION with cellobio-derived isofagomine

Structural highlights

1ocq is a 1 chain structure with sequence from Atcc 700163. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1a3h, 1e5j, 1h11, 1h2j, 1h5v, 1hf6, 1qhz, 1qi0, 1qi2, 2a3h, 3a3h, 4a3h, 5a3h, 6a3h, 7a3h, 8a3h
Activity:	Cellulase, with EC number 3.2.1.4
Resources:	FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Varrot A, Tarling CA, Macdonald JM, Stick RV, Zechel DL, Withers SG, Davies GJ. Direct observation of the protonation state of an imino sugar glycosidase inhibitor upon binding. J Am Chem Soc. 2003 Jun 25;125(25):7496-7. PMID:12812472 doi:10.1021/ja034917k

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ocq"

@@ Line 1: / Line 1: @@
-==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==
 <StructureSection load='1ocq' size='340' side='right' caption='[[1ocq]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ocq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OCQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ocq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700163 Atcc 700163]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OCQ FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IFM:5-HYDROXYMETHYL-3,4-DIHYDROXYPIPERIDINE'>IFM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a3h|1a3h]], [[1e5j|1e5j]], [[1h11|1h11]], [[1h2j|1h2j]], [[1h5v|1h5v]], [[1hf6|1hf6]], [[1qhz|1qhz]], [[1qi0|1qi0]], [[1qi2|1qi2]], [[2a3h|2a3h]], [[3a3h|3a3h]], [[4a3h|4a3h]], [[5a3h|5a3h]], [[6a3h|6a3h]], [[7a3h|7a3h]], [[8a3h|8a3h]]</td></tr>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus agaradhaerens]]
+[[Category: Atcc 700163]]
 [[Category: Cellulase]]
 [[Category: Davies, G J]]
-[[Category: Macdonald, J M]]
+[[Category: Macdonald, J]]
 [[Category: Stick, R V]]
 [[Category: Varrot, A]]

1ocq

From Proteopedia

Revision as of 08:15, 22 July 2015

COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.08 ANGSTROM RESOLUTION with cellobio-derived isofagomine

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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