PDBsum entry: 1wsa

Hydrolase

PDB id: 1wsa

Contents

Protein chains

319 a.a. *

Waters ×467

* Residue conservation analysis

PDB id:

1wsa

Name:

Hydrolase

Title:

Structure of l-asparaginase ii precursor

Structure:

Asparagine amidohydrolase. Chain: a, b. Synonym: asparaginase. Ec: 3.5.1.1

Source:

Wolinella succinogenes. Organism_taxid: 844. Atcc: 29543

Biol. unit:

Tetramer (from PDB file)

Resolution:

2.20Å R-factor: 0.158

Authors:

J.Lubkowski,G.J.Palm,G.L.Gilliland,C.Derst,K.-H.Rohm,A.Wloda

Key ref:

J.Lubkowski et al. (1996). Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginase. Eur J Biochem, 241, 201-207. PubMed id: 8898907 DOI: 10.1111/j.1432-1033.1996.0201t.x

Date:

15-Aug-96 Release date: 01-Apr-97

Protein chains

P50286  (ASPG_WOLSU) -  L-asparaginase

Seq: 330 a.a.

Struc: 319 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.5.1.1 - Asparaginase.
• Reaction: L-asparagine + H₂O = L-aspartate + NH₃

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (1 term)
• Biological process: cellular amino acid metabolic process (2 terms)
• Biochemical function: hydrolase activity (2 terms)

Added reference

DOI no: 10.1111/j.1432-1033.1996.0201t.x

Eur J Biochem 241:201-207 (1996)

PubMed id: 8898907

Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginase.

J.Lubkowski, G.J.Palm, G.L.Gilliland, C.Derst, K.H.Röhm, A.Wlodawer.

ABSTRACT

The amino acid sequence and tertiary structure of Wolinella succinogenes L-asparaginase were determined, and were compared with the structures of other type-II bacterial L-asparaginases. Each chain of this homotetrameric enzyme consists of 330 residues. The amino acid sequence is 40-50% identical to the sequences of related proteins from other bacterial sources, and all residues previously shown to be crucial for the catalytic action of these enzymes are identical. Differences between the amino acid sequence of W. succinogenes L-asparaginase and that of related enzymes are discussed in terms of the possible influence on the substrate specificity. The overall fold of the protein subunit is almost identical to that observed for other L-asparaginases. Two fragments in each subunit, a very highly flexible loop (approximately 20 amino acids) that forms part of the active site, and the N-terminus (two amino acids), are not defined in the structure. The orientation of Thr14, a residue probably involved in the catalytic activity, indicates the absence of ligand in the active-site pocket. The rigid part of the active site, which includes the asparaginase triad Thr93-Lys 166-Asp94, is structurally very highly conserved with equivalent regions found in other type-II bacterial L-asparaginases.