PDBsum entry: 1goi

Hydrolase

PDB id: 1goi

Contents

Protein chains

497 a.a. *

Ligands

GOL ×12

SO4 ×4

Waters ×1000

* Residue conservation analysis

PDB id:

1goi

Name:

Hydrolase

Title:

Crystal structure of the d140n mutant of chitinase b from serratia marcescens at 1.45 a resolution

Structure:

Chitinase b. Chain: a, b. Mutation: yes

Source:

Serratia marcescens. Organism_taxid: 615. Strain: bjl200

Biol. unit:

Dimer (from PDB file)

Resolution:

1.45Å R-factor: 0.160 R-free: 0.220

Authors:

G.Kolstad,B.Synstad,V.G.H.Eijsink,D.M.F.Van Aalten

Key ref:

G.Kolstad et al. (2002). Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution. Acta Crystallogr D Biol Crystallogr, 58, 377-379. PubMed id: 11807282 DOI: 10.1107/S0907444901018972

Date:

21-Oct-01 Release date: 15-Nov-01

Protein chains

P11797  (CHIB_SERMA) -  Chitinase B

Seq: 499 a.a.

Struc: 497 a.a.*

* PDB and UniProt seqs differ at 9 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.14 - Chitinase.
• Reaction: Hydrolysis of the 1,4-beta-linkages of N-acetyl-D-glucosamine polymers of chitin.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (1 term)
• Biological process: metabolic process (3 terms)
• Biochemical function: catalytic activity (7 terms)

DOI no: 10.1107/S0907444901018972

Acta Crystallogr D Biol Crystallogr 58:377-379 (2002)

PubMed id: 11807282

Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution.

G.Kolstad, B.Synstad, V.G.Eijsink, D.M.van Aalten.

ABSTRACT

The crystal structure of the inactive D140N mutant of Serratia marcescens was refined to 1.45 A resolution. The structure of the mutant was essentially identical to that of the wild type, with the exception of a rotation of Asp142 in the catalytic centre. In the mutant, this residue interacts with the catalytic acid (Glu144) and not with residue 140 as in the wild type. Thus, the 500-fold decrease in activity in the D140N mutant seems to be largely mediated by an effect on Asp142, confirming the crucial role of the latter residue in catalysis.

Selected figure(s)

Figure 2.
Figure 2 The DxDxE motif and the conserved residues Tyr10 and Ser93 in the ChiB D140N mutant structure (black backbone trace, side chains in stick representation). The location of the -2, -1, +1 sugar-binding subsites as observed in the complex with pentameric substrate (van Aalten et al., 2001[Aalten, D. M. F. van, Komander, D., Synstad, B., Gåseidnes, S., Peter, M. G. & Eijsink, V. G. H. (2001). Proc. Natl Acad. Sci. USA, 98, 8979-8984.]) is also shown (red stick model). In the ChiB apo structure, residue Asp142 points into the TIM barrel towards Asp140. This conformation is shown as a stick model with C atoms coloured green. The electron density (final ChiB-D140N 2|F[o]| - |F[c]|, [calc] map) around the side chains is contoured at 2.25 .

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2002, 58, 377-379) copyright 2002.

Figure was selected by an automated process.