2ix9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:55, 23 October 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2ix9.png|left|200px]]
 
-
{{STRUCTURE_2ix9| PDB=2ix9 | SCENE= }}
+
==Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A==
 +
<StructureSection load='2ix9' size='340' side='right'caption='[[2ix9]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2ix9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IX9 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2ix9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix9 OCA], [https://pdbe.org/2ix9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ix9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ix9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix9 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FAEA_ASPNG FAEA_ASPNG] Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose.<ref>PMID:9406381</ref> <ref>PMID:11931668</ref> <ref>PMID:7805053</ref> <ref>PMID:9649839</ref> <ref>PMID:11931668</ref> <ref>PMID:15081808</ref> <ref>PMID:17027758</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/ix/2ix9_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2ix9 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The thermal stability of four molecular forms (native, refolded, glycosylated, non-glycosylated) of feruloyl esterase A (FAEA) was studied. From the most to the least thermo-resistant, the four molecular species ranked as follows: (i) glycosylated form produced native, (ii) non-glycosylated form produced native, (iii) non-glycosylated form produced as inclusion bodies and refolded, and (iv) glycosylated form produced native chemically denatured and then refolded. On the basis of these results and of crystal structure data, we discuss the respective importance of protein folding and glycosylation in the thermal stability of recombinant FAEA.
-
===RESPECTIVE ROLE OF PROTEIN FOLDING AND GLYCOSYLATION IN THE THERMAL STABILITY OF RECOMBINANT FERULOYL ESTERASE A===
+
Respective importance of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase A.,Benoit I, Asther M, Sulzenbacher G, Record E, Marmuse L, Parsiegla G, Gimbert I, Asther M, Bignon C FEBS Lett. 2006 Oct 30;580(25):5815-21. Epub 2006 Sep 27. PMID:17027758<ref>PMID:17027758</ref>
-
{{ABSTRACT_PUBMED_17027758}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2ix9" style="background-color:#fffaf0;"></div>
-
[[2ix9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX9 OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:017027758</ref><references group="xtra"/>
+
</StructureSection>
[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
-
[[Category: Feruloyl esterase]]
+
[[Category: Large Structures]]
-
[[Category: Benoit, I.]]
+
[[Category: Benoit I]]
-
[[Category: Sulzenbacher, G.]]
+
[[Category: Sulzenbacher G]]
-
[[Category: Feruloyl esterase ec 3 1.1 73]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Serine esterase]]
+
-
[[Category: Xylan degradation]]
+

Current revision

Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A

PDB ID 2ix9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ix9"
Personal tools