PDBsum entry 1nal

Lyase

PDB id: 1nal

Contents

Protein chains

291 a.a. *

Ligands

SO4 ×4

Waters ×60

* Residue conservation analysis

PDB id:

1nal

Name:

Lyase

Title:

The three-dimensional structure of n-acetylneuraminate lyase from escherichia coli

Structure:

N-acetylneuraminate lyase. Chain: 1, 2, 3, 4. Ec: 4.1.3.3

Source:

Escherichia coli. Organism_taxid: 562

Biol. unit:

Tetramer (from PQS)

Resolution:

2.20Å R-factor: 0.208

Authors:

T.Izard,M.C.Lawrence,R.L.Malby,G.G.Lilley,P.M.Colman

Key ref:

T.Izard et al. (1994). The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. Structure, 2, 361-369. PubMed id: 8081752 DOI: 10.1016/S0969-2126(00)00038-1

Date:

28-Feb-94 Release date: 15-Sep-95

Protein chains

P0A6L4  (NANA_ECOLI) -  N-acetylneuraminate lyase from Escherichia coli (strain K12)

Seq: 297 a.a.

Struc: 291 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.4.1.3.3 - N-acetylneuraminate lyase.
• Reaction: aceneuramate = aldehydo-N-acetyl-D-mannosamine + pyruvate

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

Key reference

DOI no: 10.1016/S0969-2126(00)00038-1

Structure 2:361-369 (1994)

PubMed id: 8081752

The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli.

T.Izard, M.C.Lawrence, R.L.Malby, G.G.Lilley, P.M.Colman.

ABSTRACT

BACKGROUND: N-acetylneuraminate lyase catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. The enzyme plays an important role in the regulation of sialic acid metabolism in bacteria. The reverse reaction can be exploited for the synthesis of sialic acid and some of its derivatives. RESULTS: The structure of the enzyme from Escherichia coli has been determined to 2.2 A resolution by X-ray crystallography. The enzyme is shown to be a tetramer, in which each subunit consists of an alpha/beta-barrel domain followed by a carboxy-terminal extension of three alpha-helices. CONCLUSIONS: The active site of the enzyme is tentatively identified as a pocket at the carboxy-terminal end of the eight-stranded beta-barrel. Lys165 lies within this pocket and is probably the reactive residue which forms a Schiff base intermediate with the substrate. The sequence of N-acetylneuraminate lyase has similarities to those of dihydrodipicolinate synthase and MosA (an enzyme implicated in rhizopine synthesis) suggesting that these last two enzymes share a similar structure to N-acetylneuraminate lyase.

Selected figure(s)

Figure 2.
Figure 2. Stereo Cα trace of the Neu5Ac lyase monomer, viewed down the β -barrel axis from its carboxy-terminal end. Every tenth Cα is labelled. Figure 2. Stereo Cα trace of the Neu5Ac lyase monomer, viewed down the β -barrel axis from its carboxy-terminal end. Every tenth Cα is labelled. (Figure produced using MOLSCRIPT [[3]10].)

Figure 3.
Figure 3. Schematic drawing of the secondary structural elements of Neu5Ac lyase viewed down the β -barrel axis from its carboxy- terminal end. The putative catalytic residue Lys165 (see text) is shown in ball-and-stick representation. Figure 3. Schematic drawing of the secondary structural elements of Neu5Ac lyase viewed down the β -barrel axis from its carboxy- terminal end. The putative catalytic residue Lys165 (see text) is shown in ball-and-stick representation. (Figure produced using MOLSCRIPT [[3]10].)

The above figures are reprinted by permission from Cell Press: Structure (1994, 2, 361-369) copyright 1994.

Figures were selected by an automated process.