PDBsum entry 2ea3

Hydrolase

PDB id: 2ea3

Contents

Protein chain

183 a.a. *

Ligands

SO4 ×3

Waters ×58

* Residue conservation analysis

PDB id:

2ea3

Name:

Hydrolase

Title:

Crystal structure of cellulomonas bogoriensis chymotrypsin

Structure:

Chymotrypsin. Chain: a. Ec: 3.4.21.-

Source:

Cellulomonas bogoriensis. Organism_taxid: 301388

Resolution:

1.78Å R-factor: 0.167 R-free: 0.195

Authors:

A.Shaw,R.Bott

Key ref:

A.Shaw et al. (2007). Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 266-269. PubMed id: 17401191 DOI: 10.1107/S1744309107008937

Date:

30-Jan-07 Release date: 24-Apr-07

Protein chain

A2RQE2  (A2RQE2_9CELL) -  Preprocellulomonadin from Cellulomonas bogoriensis

Seq: 495 a.a.

Struc: 183 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.21.- - ?????

DOI no: 10.1107/S1744309107008937

Acta Crystallogr Sect F Struct Biol Cryst Commun 63:266-269 (2007)

PubMed id: 17401191

Structure determination and analysis of a bacterial chymotrypsin from Cellulomonas bogoriensis.

A.Shaw, M.L.Saldajeno, M.A.Kolkman, B.E.Jones, R.Bott.

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.

Selected figure(s)

Figure 1.
(a) Crystals of cellulomonadin. (b) 2F [o] [minus sign] F [c] electron density of cellulomonadin around the catalytic triad, contoured at 1[sigma]. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 April 1; 63(Pt 4): 266–269. Published online 2007 March 23. doi: 10.1107/S1744309107008937. Copyright [copyright] International Union of Crystallography 2007

Figure 2.
Structure of cellulomonadin. (a) Topology diagram of cellulomonadin. [beta]-Sheets are shown as blue arrows pointing in the direction from the N-terminal to the C-terminal ends. [alpha]-Helices are shown as red cylinders. Connections between secondary-structure elements are shown as black line arrows. (b) Tertiary structure of cellulomonadin. The catalytic triad residues His32, Asp56 and Ser137 are shown as ball-and-stick representations. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 April 1; 63(Pt 4): 266–269. Published online 2007 March 23. doi: 10.1107/S1744309107008937. Copyright [copyright] International Union of Crystallography 2007

The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr Sect F Struct Biol Cryst Commun (2007, 63, 266-269) copyright 2007.

Figures were selected by an automated process.