1KKO

CRYSTAL STRUCTURE OF CITROBACTER AMALONATICUS METHYLASPARTATE AMMONIA LYASE

PDB DOI: https://doi.org/10.2210/pdb1KKO/pdb

Classification: LYASE
Organism(s): Citrobacter amalonaticus
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2001-12-10 Released: 2002-01-30
Deposition Author(s): Levy, C.W., Buckley, P.A., Sedelnikova, S., Kato, Y., Asano, Y., Rice, D.W., Baker, P.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.33 Å
R-Value Free: 0.191
R-Value Work: 0.161
R-Value Observed: 0.162

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase.

Levy, C.W., Buckley, P.A., Sedelnikova, S., Kato, Y., Asano, Y., Rice, D.W., Baker, P.J.

(2002) Structure 10: 105-113

PubMed: 11796115 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(01)00696-7
Primary Citation of Related Structures:
1KKO, 1KKR

PubMed Abstract:
Methylaspartate ammonia lyase (MAL) catalyzes the magnesium-dependent reversible alpha,beta-elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to mesaconic acid. The 1.3 A MAD crystal structure of the dimeric Citrobacter amalonaticus MAL shows that each subunit comprises two domains, one of which adopts the classical TIM barrel fold, with the active site at the C-terminal end of the barrel. Despite very low sequence similarity, the structure of MAL is closely related to those of representative members of the enolase superfamily, indicating that the mechanism of MAL involves the initial abstraction of a proton alpha to the 3-carboxyl of (2S,3S)-3-methylasparic acid to yield an enolic intermediate. This analysis resolves the conflict that had linked MAL to the histidine and phenylalanine ammonia lyase family of enzymes.

Organizational Affiliation

Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, United Kingdom.

Macromolecule Content

Total Structure Weight: 92.08 kDa
Atom Count: 8,530
Modelled Residue Count: 822
Deposited Residue Count: 826
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
3-METHYLASPARTATE AMMONIA-LYASE	A, B	413	Citrobacter amalonaticus	Mutation(s): 10 Gene Names: MAL EC: 4.3.1.2
UniProt
Find proteins for O66145 (Citrobacter amalonaticus) Explore O66145 Go to UniProtKB: O66145
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O66145
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A]	C [auth A]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain C [auth A]