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2cnc

From Proteopedia

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Family 10 xylanase

Structural highlights

2cnc is a 1 chain structure with sequence from Cellvibrio mixtus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O68541_9GAMM

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

Thermostability is an important property of industrially significant hydrolytic enzymes: understanding the structural basis for this attribute will underpin the future biotechnological exploitation of these biocatalysts. The Cellvibrio family 10 (GH10) xylanases display considerable sequence identity but exhibit significant differences in thermostability; thus, these enzymes represent excellent models to examine the structural basis for the variation in stability displayed by these glycoside hydrolases. Here, we have subjected the intracellular Cellvibrio mixtus xylanase CmXyn10B to forced protein evolution. Error-prone PCR and selection identified a double mutant, A334V/G348D, which confers an increase in thermostability. The mutant has a Tm 8 degrees C higher than the wild-type enzyme and, at 55 degrees C, the first-order rate constant for thermal inactivation of A334V/G348D is 4.1 x 10(-4) min(-1), compared to a value of 1.6 x 10(-1) min(-1) for the wild-type enzyme. The introduction of the N to C-terminal disulphide bridge into A334V/G348D, which increases the thermostability of wild-type CmXyn10B, conferred a further approximately 2 degrees C increase in the Tm of the double mutant. The crystal structure of A334V/G348D showed that the introduction of Val334 fills a cavity within the hydrophobic core of the xylanase, increasing the number of van der Waals interactions with the surrounding aromatic residues, while O(delta1) of Asp348 makes an additional hydrogen bond with the amide of Gly344 and O(delta2) interacts with the arabinofuranose side-chain of the xylose moiety at the -2 subsite. To investigate the importance of xylan decorations in productive substrate binding, the activity of wild-type CmXyn10B, the mutant A334V/G348D, and several other GH10 xylanases against xylotriose and xylotriose containing an arabinofuranose side-chain (AX3) was assessed. The enzymes were more active against AX3 than xylotriose, providing evidence that the arabinose side-chain makes a generic contribution to substrate recognition by GH10 xylanases.

Probing the structural basis for the difference in thermostability displayed by family 10 xylanases.,Xie H, Flint J, Vardakou M, Lakey JH, Lewis RJ, Gilbert HJ, Dumon C J Mol Biol. 2006 Jun 30;360(1):157-67. Epub 2006 May 15. PMID:16762367^[1]

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

References

↑ Xie H, Flint J, Vardakou M, Lakey JH, Lewis RJ, Gilbert HJ, Dumon C. Probing the structural basis for the difference in thermostability displayed by family 10 xylanases. J Mol Biol. 2006 Jun 30;360(1):157-67. Epub 2006 May 15. PMID:16762367 doi:10.1016/j.jmb.2006.05.002

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/2cnc"

@@ Line 1: / Line 1: @@
-==FAMILY 10 XYLANASE==
-<StructureSection load='2cnc' size='340' side='right' caption='[[2cnc]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+==Family 10 xylanase==
+<StructureSection load='2cnc' size='340' side='right'caption='[[2cnc]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2cnc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cellvibrio_mixtus Cellvibrio mixtus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CNC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2cnc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_mixtus Cellvibrio mixtus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CNC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene>, <scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</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]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1uqy|1uqy]], [[1uqz|1uqz]], [[1ur1|1ur1]], [[1ur2|1ur2]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</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=2cnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cnc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cnc RCSB], [http://www.ebi.ac.uk/pdbsum/2cnc PDBsum]</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=2cnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cnc OCA], [https://pdbe.org/2cnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cnc RCSB], [https://www.ebi.ac.uk/pdbsum/2cnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cnc ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/O68541_9GAMM O68541_9GAMM]
 == 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/cn/2cnc_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/2cnc_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].
+</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/main_output.php?pdb_ID=2cnc ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2cnc" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 30: / Line 34: @@
 </StructureSection>
 [[Category: Cellvibrio mixtus]]
-[[Category: Dumon, C]]
+[[Category: Large Structures]]
-[[Category: Flint, J]]
+[[Category: Dumon C]]
-[[Category: Gilbert, H J]]
+[[Category: Flint J]]
-[[Category: Lakey, J H]]
+[[Category: Gilbert HJ]]
-[[Category: Lewis, R J]]
+[[Category: Lakey JH]]
-[[Category: Vardakou, M]]
+[[Category: Lewis RJ]]
-[[Category: Xie, H]]
+[[Category: Vardakou M]]
-[[Category: Decorated sugar]]
+[[Category: Xie H]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Thermostability]]
-[[Category: Xylan degradation]]
-[[Category: Xylanase]]

2cnc

From Proteopedia

Current revision

Family 10 xylanase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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