PDBsum entry: 1o7j

Hydrolase

PDB-id: 1o7j

Biological unit = asymmetric unit,
as shown
(as defined in PDB file)

Contents

Description

Header details

Header records

References

PROCHECK

Protein chains

325 a.a. *

Ligands

SO4 ×8

GOL ×2

EDO-EDO-EDO-EDO-EDO

EDO-EDO-EDO

EDO-EDO-EDO-EDO

Waters ×1360

* Residue conservation analysis

Tools

Clefts Calculation

PDB id:

1o7j

Name:

Hydrolase

Title:

Atomic resolution structure of erwinia chrysanthemi l-asparaginase

Structure:

L-asparaginase. Chain: a, b, c, d. Synonym: l-asparagine amidohydrolase, l-asnase. Ec: 3.5.1.1

Source:

Erwinia chrysanthemi. Organism_taxid: 556

Biological unit:

Tetramer (from PDB file)

UniProt:

Chains A, B, C, D: P06608 (ASPG_ERWCH)

Seq:

Struc:

Seq:

348 a.a.

Struc:

325 a.a.*

Key:	PfamA domain
Secondary structure	CATH domain

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme class:

E.C.3.5.1.1   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:

L-asparagine + H₂O = L-aspartate + NH₃ (see diagram below)

Resolution:

1.0Å

R-factor:

0.109

R-free:

0.128

Authors:

J.Lubkowski,M.Dauter,K.Aghaiypour,A.Wlodawer,Z.Dauter

Key ref:

J.Lubkowski et al. (2003). Atomic resolution structure of Erwinia chrysanthemi L-asparaginase.. Acta Crystallogr D Biol Crystallogr, 59, 84-92. [PubMed id: 12499544] [DOI: 10.1107/S0907444902019443]

Date:

07-Nov-02

Release date:

04-Dec-02

Related entries:

1hfj asparaginase from erwinia chrysanthemi, hexagonal form with sulfate
1hfk asparaginase from erwinia chrysanthemi, hexagonal form with partial sulfate
1hfw x-ray structure of the complex between erwinia chrysanthemi l-asparaginase and l- glutamate
1hg0 x-ray structure of the complex between erwinia chrysanthemi l-asparaginase and succinic acid
1hg1 x-ray structure of the complex between erwinia chrysanthemi l-asparaginase and d- aspartate
1jsl crystal structure of erwinia chrysanthemi l- asparaginasecomplexed with 6-hydroxy-d- norleucine
1jsr crystal structure of erwinia chrysanthemi l- asparaginasecomplexed with 6-hydroxy-l- norleucine

Quick_links

Procheck

Surface

Key reference

DOI no: 10.1107/S0907444902019443

Acta Crystallogr D Biol Crystallogr 59:84-92 (2003)

PubMed id: 12499544

Atomic resolution structure of Erwinia chrysanthemi L-asparaginase.

J.Lubkowski, M.Dauter, K.Aghaiypour, A.Wlodawer, Z.Dauter.

ABSTRACT

An X-ray structure of L-asparaginase from Erwinia chrysanthemi (ErA) has been refined at 1 A resolution to an R factor of below 0.1, using data collected on a synchrotron source. With four molecules of the enzyme consisting of 327 amino acids each, this crystal contains one of the largest asymmetric units of a protein refined to date at atomic resolution. Previously, structures of ErA and of related enzymes from other bacterial sources have been refined at resolutions not exceeding 1.7 A; thus, the present structure represents a very significant improvement in the quality of the available models of these proteins and should provide a good basis for future studies of the conformational variability of proteins, identification of subtle conformational features and corroboration of the stereochemical libraries, amongst other things. L-Asparaginases, which are enzymes that catalyze the hydrolysis of L-asparagine to aspartic acid, have been used for over 30 y as therapeutic agents in the treatment of acute childhood lymphoblastic leukemia, although the details of the enzymatic reaction and substrate specificity have not yet been completely elucidated. This atomic resolution structure is a step in that direction.