2ix9

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[[Image:2ix9.jpg|left|200px]]
[[Image:2ix9.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2ix9 |SIZE=350|CAPTION= <scene name='initialview01'>2ix9</scene>, resolution 1.70&Aring;
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The line below this paragraph, containing "STRUCTURE_2ix9", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Feruloyl_esterase Feruloyl esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.73 3.1.1.73] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2ix9| PDB=2ix9 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ix9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix9 OCA], [http://www.ebi.ac.uk/pdbsum/2ix9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ix9 RCSB]</span>
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}}
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'''RESPECTIVE ROLE OF PROTEIN FOLDING AND GLYCOSYLATION IN THE THERMAL STABILITY OF RECOMBINANT FERULOYL ESTERASE A'''
'''RESPECTIVE ROLE OF PROTEIN FOLDING AND GLYCOSYLATION IN THE THERMAL STABILITY OF RECOMBINANT FERULOYL ESTERASE A'''
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[[Category: Benoit, I.]]
[[Category: Benoit, I.]]
[[Category: Sulzenbacher, G.]]
[[Category: Sulzenbacher, G.]]
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[[Category: feruloyl esterase ec 3 1.1 73]]
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[[Category: Feruloyl esterase ec 3 1.1 73]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: serine esterase]]
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[[Category: Serine esterase]]
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[[Category: xylan degradation]]
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[[Category: Xylan degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:01:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:56 2008''
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Revision as of 05:01, 4 May 2008

Image:2ix9.jpg

Template:STRUCTURE 2ix9

RESPECTIVE ROLE OF PROTEIN FOLDING AND GLYCOSYLATION IN THE THERMAL STABILITY OF RECOMBINANT FERULOYL ESTERASE A


Overview

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.

About this Structure

2IX9 is a Single protein structure of sequence from Aspergillus niger. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 08:01:48 2008

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