2ix9
From Proteopedia
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| - | [[Image:2ix9.jpg|left|200px]]<br /><applet load="2ix9" size=" | + | [[Image:2ix9.jpg|left|200px]]<br /><applet load="2ix9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ix9, resolution 1.70Å" /> | caption="2ix9, resolution 1.70Å" /> | ||
'''RESPECTIVE ROLE OF PROTEIN FOLDING AND GLYCOSYLATION IN THE THERMAL STABILITY OF RECOMBINANT FERULOYL ESTERASE A'''<br /> | '''RESPECTIVE ROLE OF PROTEIN FOLDING AND GLYCOSYLATION IN THE THERMAL STABILITY OF RECOMBINANT FERULOYL ESTERASE A'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IX9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] with SO4, CXS and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2IX9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CXS:'>CXS</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylan degradation]] | [[Category: xylan degradation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:39:17 2008'' |
Revision as of 08:39, 3 February 2008
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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 with , and as ligands. Active as Feruloyl esterase, with EC number 3.1.1.73 Known structural/functional Site: . 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
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