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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 63 266-9 (2007)
Cited: 3 times
EuropePMC logo PMID: 17401191

Abstract

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.

Articles - 2ea3 mentioned but not cited (3)

  1. A New DelPhi Feature for Modeling Electrostatic Potential around Proteins: Role of Bound Ions and Implications for Zeta-Potential. Chakravorty A, Jia Z, Li L, Alexov E. Langmuir 33 2283-2295 (2017)
  2. Protein surface representation and analysis by dimension reduction. Yang H, Qureshi R, Sacan A. Proteome Sci 10 Suppl 1 S1 (2012)
  3. 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 63 266-269 (2007)




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