2ix9
From Proteopedia
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|PDB= 2ix9 |SIZE=350|CAPTION= <scene name='initialview01'>2ix9</scene>, resolution 1.70Å | |PDB= 2ix9 |SIZE=350|CAPTION= <scene name='initialview01'>2ix9</scene>, resolution 1.70Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= | + | |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> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Benoit, I.]] | [[Category: Benoit, I.]] | ||
[[Category: Sulzenbacher, G.]] | [[Category: Sulzenbacher, G.]] | ||
| - | [[Category: CXS]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: SO4]] | ||
[[Category: feruloyl esterase ec 3 1.1 73]] | [[Category: feruloyl esterase ec 3 1.1 73]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: xylan degradation]] | [[Category: xylan degradation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:49:56 2008'' |
Revision as of 00:49, 31 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , | ||||||
| Activity: | Feruloyl esterase, with EC number 3.1.1.73 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 03:49:56 2008
