1ly8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1ly8.jpg|left|200px]] | [[Image:1ly8.jpg|left|200px]] | ||
'''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== | ||
| Line 7: | Line 16: | ||
==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]] | ||
| Line 31: | Line 40: | ||
[[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
| |||||||||||||
| 1ly8, resolution 2.05Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | NAG, BMA, MAN, CA, HEM and GOL | ||||||||||||
| 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
