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1ly8
From Proteopedia
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| - | [[Image:1ly8.jpg|left|200px]] | + | [[Image:1ly8.jpg|left|200px]] |
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| - | '''The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures''' | + | {{Structure |
| + | |PDB= 1ly8 |SIZE=350|CAPTION= <scene name='initialview01'>1ly8</scene>, resolution 2.05Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] | ||
| + | |GENE= CIP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5346 Coprinopsis cinerea]) | ||
| + | }} | ||
| + | |||
| + | '''The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LY8 is a [ | + | 1LY8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Coprinopsis_cinerea Coprinopsis cinerea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LY8 OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability., Houborg K, Harris P, Poulsen JC, Schneider P, Svendsen A, Larsen S, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):997-1003. Epub 2003, May 23. PMID:[http:// | + | The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability., Houborg K, Harris P, Poulsen JC, Schneider P, Svendsen A, Larsen S, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):997-1003. Epub 2003, May 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12777761 12777761] |
[[Category: Coprinopsis cinerea]] | [[Category: Coprinopsis cinerea]] | ||
[[Category: Peroxidase]] | [[Category: Peroxidase]] | ||
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[[Category: thermostability]] | [[Category: thermostability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:36:32 2008'' |
Revision as of 10:36, 20 March 2008
| |||||||
| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , and | ||||||
| Gene: | CIP1 (Coprinopsis cinerea) | ||||||
| Activity: | Peroxidase, with EC number 1.11.1.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability and insight into modelling of protein structures
Overview
Seven amino-acid substitutions introduced into the 343 amino-acid-long sequence of Coprinus cinereus peroxidase (CiP) led to a mutant enzyme (TS-rCiP) which is more stable than the native enzyme at higher temperature, pH and hydrogen peroxide concentrations. It is therefore more suitable for industrial applications. A structure determination was conducted on a deglycosylated but still active form of TS-rCiP based on X-ray diffraction data to 2.05 A resolution measured on a crystal cooled to 100 K and refined to R = 0.202 and R(free) = 0.249. The increased stability of the TS-rCiP enzyme can be understood from the structural changes of the TS-rCiP structure revealed by a comparative analysis with other known CiP structures. One of the more significant changes caused by three of the substitutions, I49S, V53A and T121A, is the conversion of a hydrophobic pocket into a hydrophilic pocket with associated changes in the water structure and the hydrogen-bonding interactions. The E239G substitution, which gives rise to increased thermostability at high pH, creates changes in the water structure and in the orientation of a phenylalanine (Phe236) in its vicinity. The three substitutions M166F, M242 and Y242F introduced to increase the oxidative stability do not introduce any structural changes.
About this Structure
1LY8 is a Single protein structure of sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA.
Reference
The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability., Houborg K, Harris P, Poulsen JC, Schneider P, Svendsen A, Larsen S, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):997-1003. Epub 2003, May 23. PMID:12777761
Page seeded by OCA on Thu Mar 20 12:36:32 2008
Categories: Coprinopsis cinerea | Peroxidase | Single protein | Harris, P. | Houborg, K. | Larsen, S. | Poulsen, J C.N. | Schneider, P. | Svendsen, A. | BMA | CA | GOL | HEM | MAN | NAG | Coprinus cinereus | Mutant | Thermostability
