Sandbox UNLPam 7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:45, 9 December 2015) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
== Crystal structure of a novel two domain GH78 family a-rhamnosidase from Klebsiella
+
== Crystal structure of a novel two domain GH78 family a-rhamnosidase from Klebsiella oxytoca with rhamnose bound ==
-
oxytoca with rhamnose bound ==
+
-
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
+
-
== Structure ==
+
-
The crystal structure of the GH78 family a-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 A °
+
-
resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is
+
-
preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This
+
-
KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures.
+
-
Nevertheless, the enzyme displays a-rhamnosidase activity when assayed in vitro, suggesting that the additional structural
+
-
domains found in the related enzymes are dispensible for function.
+
-
== Function ==
+
==Introduction==
-
a-L-rhamnose is found in plants and bacteria
+
<StructureSection load='4xhc' size='350' side='right' caption='X-ray crystal structure of the a-L-rhamnosidase from K. oxytoca (KoRha).' scene='71/719552/4xhc_1/1'>4xhc structure</scene>'>
 +
 
 +
 
 +
a-L-rhamnosidases (E.C. 3.2.1.40) are found widely distributed
 +
in nature and have been reported in animals,
 +
plants, yeast, fungi and bacteria, where they are responsible
 +
for the cleavage of a-L-rhamnose from a wide range of
 +
compounds.1 a-L-rhamnose is found in plants and bacteria
as components of polysaccharides, such as pectins,2 and
as components of polysaccharides, such as pectins,2 and
the O antigen polysaccharides, responsible for determining
the O antigen polysaccharides, responsible for determining
Line 20: Line 18:
and for the release of flavonoids from rhamnosylated precursors;
and for the release of flavonoids from rhamnosylated precursors;
in wine production they play a role in the hydrolysis
in wine production they play a role in the hydrolysis
-
of glycosylated terpene aroma compounds.5 In the
+
of glycosylated terpene aroma compounds.
-
context of expanding and diversifying the suite of enzymes
+
-
available to us for carbohydrate biotransformations,6–13 we
+
-
were drawn to consider a-rhamnosidases.
+
-
In the CAZy database,14 rhamnosidases are currently
+
-
classified into GH28 pectin hydrolases, GH78 containing
+
-
exclusively rhamnosidases, and GH106 containing a single enzyme from Sphingomonas
+
-
 
+
-
== Disease ==
+
-
 
+
-
== Relevance ==
+
-
 
+
-
== Structural highlights ==
+
-
 
+
-
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
+
 +
==KoRha structure==
 +
The crystal structure of KoRha with rhamnose bound was
 +
determined to 2.7A ° resolution. The final model consisted of
 +
two KoRha subunits related by a non-crystallographic twofold
 +
axis (giving a corresponding solvent content of 73%) in
 +
the asymmetric unit, with each monomer containing a
 +
bound rhamnose. Dynamic light scattering had suggested
 +
that KoRha was a homodimer in solution and the structure
 +
of KoRha confirmed this, giving a dimer interface of 1389.9
 +
A °
 +
2 (as calculated using the PISA server (http://www.ebi.ac.
 +
uk/pdbe/pisa/).
 +
Each monomer of KoRha is composed of two
 +
domains. Domain A, the catalytic domain, is mainly ahelical,
 +
consisting of residues 11–30 and 180–523, and
 +
contains the bound rhamnose. Domain B, the dimerization
 +
domain, is a b-sandwich domain consisting of residues
 +
31–179.
 +
<scene name='71/719552/4xhc_1/1'>4xhc structure</scene>
</StructureSection>
</StructureSection>
-
== References ==
 
-
<references/>
 

Current revision

Crystal structure of a novel two domain GH78 family a-rhamnosidase from Klebsiella oxytoca with rhamnose bound

Introduction

X-ray crystal structure of the a-L-rhamnosidase from K. oxytoca (KoRha).

Drag the structure with the mouse to rotate
Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_UNLPam_7"
Personal tools