2vzt

From Proteopedia

(Difference between revisions)

Current revision

Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine

Structural highlights

2vzt is a 2 chain structure with sequence from Amycolatopsis orientalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EBDG_AMYOR Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.^[1] ^[2]

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

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.

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^[3]

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

References

↑ Cote N, Fleury A, Dumont-Blanchette E, Fukamizo T, Mitsutomi M, Brzezinski R. Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases. Biochem J. 2006 Mar 15;394(Pt 3):675-86. PMID:16316314 doi:http://dx.doi.org/10.1042/BJ20051436
↑ Nanjo F, Katsumi R, Sakai K. Purification and characterization of an exo-beta-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis. J Biol Chem. 1990 Jun 15;265(17):10088-94. PMID:2351651
↑ van Bueren AL, Ghinet MG, Gregg K, Fleury A, Brzezinski R, Boraston AB. The structural basis of substrate recognition in an exo-beta-D-glucosaminidase involved in chitosan hydrolysis. J Mol Biol. 2009 Jan 9;385(1):131-9. Epub 2008 Oct 19. PMID:18976664 doi:10.1016/j.jmb.2008.10.031

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/2vzt"

@@ Line 1: / Line 1: @@
-==COMPLEX OF AMYCOLATOPSIS ORIENTALIS EXO-CHITOSANASE CSXA E541A WITH PNP-BETA-D-GLUCOSAMINE==
+==Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine==
-<StructureSection load='2vzt' size='340' side='right' caption='[[2vzt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='2vzt' size='340' side='right'caption='[[2vzt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vzt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_orientalis"_pittenger_and_brigham_1956 "streptomyces orientalis" pittenger and brigham 1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VZT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vzt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_orientalis Amycolatopsis orientalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VZT FirstGlance]. <br>
-</td></tr><tr id='ligand'><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></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vzo|2vzo]], [[2vzp|2vzp]], [[2vzq|2vzq]], [[2vzr|2vzr]], [[2vzs|2vzs]], [[2vzu|2vzu]], [[2vzv|2vzv]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzt OCA], [http://pdbe.org/2vzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vzt RCSB], [http://www.ebi.ac.uk/pdbsum/2vzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vzt ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzt OCA], [https://pdbe.org/2vzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vzt RCSB], [https://www.ebi.ac.uk/pdbsum/2vzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vzt ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/EBDG_AMYOR EBDG_AMYOR] Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.<ref>PMID:16316314</ref> <ref>PMID:2351651</ref>
 == 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/2vzt_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vz/2vzt_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 31: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Streptomyces orientalis pittenger and brigham 1956]]
+[[Category: Amycolatopsis orientalis]]
-[[Category: Boraston, A B]]
+[[Category: Large Structures]]
-[[Category: Brzezinski, R]]
+[[Category: Boraston AB]]
-[[Category: Bueren, A Lammerts Van]]
+[[Category: Brzezinski R]]
-[[Category: Fleury, A]]
+[[Category: Fleury A]]
-[[Category: Ghinet, M G]]
+[[Category: Ghinet MG]]
-[[Category: Gregg, K]]
+[[Category: Gregg K]]
-[[Category: Csxa]]
+[[Category: Lammerts van Bueren A]]
-[[Category: Exo-beta-d-glucosaminidase]]
-[[Category: Gh2]]
-[[Category: Glycoside hydrolase]]
-[[Category: Hydrolase]]
-[[Category: Pnp-glucosamine]]

2vzt

From Proteopedia

Current revision

Complex of Amycolatopsis orientalis exo-chitosanase CsxA E541A with PNP-beta-D-glucosamine

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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