2vzu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2vzu" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:2vzu.png|left|200px]]
+
==COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA D469A WITH PNP-BETA-D-GLUCOSAMINE==
 +
<StructureSection load='2vzu' size='340' side='right' caption='[[2vzu]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2vzu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VZU FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=PNJ:PNP-BETA-D-GLUCOSAMINE'>PNJ</scene><br>
 +
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vzo|2vzo]], [[2vzp|2vzp]], [[2vzq|2vzq]], [[2vzr|2vzr]], [[2vzs|2vzs]], [[2vzt|2vzt]], [[2vzv|2vzv]]</td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vzu RCSB], [http://www.ebi.ac.uk/pdbsum/2vzu PDBsum]</span></td></tr>
 +
<table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/2vzu_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Family 2 of the glycoside hydrolase classification is one of the largest families. Structurally characterized members of this family include enzymes with beta-galactosidase activity (Escherichia coli LacZ), beta-glucuronidase activity (Homo sapiens GusB), and beta-mannosidase activity (Bacteroides thetaiotaomicron BtMan2A). Here, we describe the structure of a family 2 glycoside hydrolase, CsxA, from Amycolatopsis orientalis that has exo-beta-D-glucosaminidase (exo-chitosanase) activity. Analysis of a product complex (1.85 A resolution) reveals a unique negatively charged pocket that specifically accommodates the nitrogen of nonreducing end glucosamine residues, allowing this enzyme to discriminate between glucose and glucosamine. This also provides structural evidence for the role of E541 as the catalytic nucleophile and D469 as the catalytic acid/base. The structures of an E541A mutant in complex with a natural beta-1,4-D-glucosamine tetrasaccharide substrate and both E541A and D469A mutants in complex with a pNP-beta-D-glucosaminide synthetic substrate provide insight into interactions in the +1 subsite of this enzyme. Overall, a comparison with the active sites of other GH2 enzymes highlights the unique architecture of the CsxA active site, which imparts specificity for its cationic substrate.
-
{{STRUCTURE_2vzu| PDB=2vzu | SCENE= }}
+
The structural basis of substrate recognition in an exo-beta-D-glucosaminidase involved in chitosan hydrolysis.,van Bueren AL, Ghinet MG, Gregg K, Fleury A, Brzezinski R, Boraston AB J Mol Biol. 2009 Jan 9;385(1):131-9. Epub 2008 Oct 19. PMID:18976664<ref>PMID:18976664</ref>
-
===COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA D469A WITH PNP-BETA-D-GLUCOSAMINE===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_18976664}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[2vzu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZU OCA].
+
</StructureSection>
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:018976664</ref><references group="xtra"/>
+
[[Category: Amycolatopsis orientalis]]
[[Category: Amycolatopsis orientalis]]
[[Category: Boraston, A B.]]
[[Category: Boraston, A B.]]

Revision as of 01:20, 1 October 2014

COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA D469A WITH PNP-BETA-D-GLUCOSAMINE

2vzu, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Views
Personal tools
Navigation
Toolbox