2ea3
From Proteopedia
(New page: 200px<br /><applet load="2ea3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ea3, resolution 1.78Å" /> '''Crystal Structure Of...) |
|||
Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
- | The crystal structure of a secreted chymotrypsin from the alkaliphile | + | The crystal structure of a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis has been determined using data to 1.78 A resolution and refined to a crystallographic R factor of 0.167. The crystal structure reveals a large P1 substrate-specificity pocket, as expected for chymotrypsins. The structure is compared with close structural homologues. This comparison does not reveal clear reasons for the alkali tolerance of the enzyme, but the greater compactness of the structure and lowered hydrogen bonding may play a role. |
==About this Structure== | ==About this Structure== | ||
Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
- | Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis., Shaw A, Saldajeno ML, Kolkman MA, Jones BE, Bott R, Acta | + | Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis., Shaw A, Saldajeno ML, Kolkman MA, Jones BE, Bott R, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):266-9. Epub 2007 Mar 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17401191 17401191] |
[[Category: Cellulomonas bogoriensis]] | [[Category: Cellulomonas bogoriensis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
Line 20: | Line 20: | ||
[[Category: protease]] | [[Category: protease]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:07:51 2008'' |
Revision as of 15:07, 21 February 2008
|
Crystal Structure Of Cellulomonas Bogoriensis Chymotrypsin
Overview
The crystal structure of a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis has been determined using data to 1.78 A resolution and refined to a crystallographic R factor of 0.167. The crystal structure reveals a large P1 substrate-specificity pocket, as expected for chymotrypsins. The structure is compared with close structural homologues. This comparison does not reveal clear reasons for the alkali tolerance of the enzyme, but the greater compactness of the structure and lowered hydrogen bonding may play a role.
About this Structure
2EA3 is a Protein complex structure of sequences from Cellulomonas bogoriensis with as ligand. Full crystallographic information is available from OCA.
Reference
Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis., Shaw A, Saldajeno ML, Kolkman MA, Jones BE, Bott R, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Apr 1;63(Pt, 4):266-9. Epub 2007 Mar 23. PMID:17401191
Page seeded by OCA on Thu Feb 21 17:07:51 2008