2wyn

From Proteopedia

(Difference between revisions)

@@ Line 1: / Line 1: @@
-==STRUCTURE OF FAMILY 37 TREHALASE FROM ESCHERICHIA COLI IN COMPLEX WITH A CASUARINE-6-O-A-D-GLUCOSIDE ANALOGUE==
+==Structure of family 37 trehalase from Escherichia coli in complex with a casuarine-6-O-a-D-glucoside analogue==
 <StructureSection load='2wyn' size='340' side='right' caption='[[2wyn]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
@@ Line 15: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wy/2wyn_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wy/2wyn_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 09:42, 3 October 2018

Structure of family 37 trehalase from Escherichia coli in complex with a casuarine-6-O-a-D-glucoside analogue

spinqualitylabelsall models

2wyn, resolution 2.10Å

Show:Asymmetric Unit Biological Assembly

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Structural highlights

2wyn is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	2jjb, 2jg0, 2jf4
Activity:	Alpha,alpha-trehalase, with EC number 3.2.1.28
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TREA_ECOLI] Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.[HAMAP-Rule:MF_01060]

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

Two novel casuarine-6-alpha-D-glucoside analogues, as well as the parent compound, were synthesized and tested as inhibitors towards Chironomus riparius, mammalian pig kidney and Escherichia coli trehalases. Their potent and selective activity is promising for the development of new insecticides.

Casuarine-6-O-alpha-D-glucoside and its analogues are tight binding inhibitors of insect and bacterial trehalases.,Cardona F, Goti A, Parmeggiani C, Parenti P, Forcella M, Fusi P, Cipolla L, Roberts SM, Davies GJ, Gloster TM Chem Commun (Camb). 2010 Apr 21;46(15):2629-31. PMID:20461849^[1]

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

References

↑ Cardona F, Goti A, Parmeggiani C, Parenti P, Forcella M, Fusi P, Cipolla L, Roberts SM, Davies GJ, Gloster TM. Casuarine-6-O-alpha-D-glucoside and its analogues are tight binding inhibitors of insect and bacterial trehalases. Chem Commun (Camb). 2010 Apr 21;46(15):2629-31. PMID:20461849

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wyn"

2wyn

From Proteopedia

Revision as of 09:42, 3 October 2018

Structure of family 37 trehalase from Escherichia coli in complex with a casuarine-6-O-a-D-glucoside analogue

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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