PDBsum entry 1a2v

Amine oxidase

PDB id: 1a2v

Contents

Protein chains

(+ 0 more) 655 a.a. *

Metals

_CU ×6

Waters ×2556

* Residue conservation analysis

PDB id:

1a2v

Name:

Amine oxidase

Title:

Copper amine oxidase from hansenula polymorpha

Structure:

Methylamine oxidase. Chain: a, b, c, d, e, f. Engineered: yes

Source:

Pichia angusta. Organism_taxid: 4905. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932

Biol. unit:

Dimer (from PDB file)

Resolution:

2.40Å R-factor: 0.184 R-free: 0.224

Authors:

R.Li,F.S.Mathews

Key ref:

R.Li et al. (1997). Crystallographic study of yeast copper amine oxidase. Acta Crystallogr D Biol Crystallogr, 53, 364-370. PubMed id: 15299901 DOI: 10.1107/S0907444997000814

Date:

12-Jan-98 Release date: 27-May-98

Protein chains

P12807  (AMO_PICAN) -  Peroxisomal primary amine oxidase from Pichia angusta

Seq: 692 a.a.

Struc: 655 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.1.4.3.21 - primary-amine oxidase.
• Reaction: a primary methyl amine + O2 + H2O = an aldehyde + H2O2 + NH4⁺

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

reference

DOI no: 10.1107/S0907444997000814

Acta Crystallogr D Biol Crystallogr 53:364-370 (1997)

PubMed id: 15299901

Crystallographic study of yeast copper amine oxidase.

R.Li, L.Chen, D.Cai, J.P.Klinman, F.S.Mathews.

ABSTRACT

The copper-containing amine oxidase from the yeast Hansenula polymorpha (YAO) has been crystallized and partially solved by molecular replacement. It catalyzes the oxidative deamination of primary amines by molecular oxygen to the corresponding aldehydes, ammonia and hydrogen peroxide. It contains a covalently bound redox cofactor, topa quinone, generated by post-translational modification of a single tyrosine side chain. The crystals of YAO are orthorhombic, with space-group symmetry P2(1)2(1)2(1) and unit-cell dimensions a = 138.8, b = 148.2, c = 234.0 A and diffract X-rays beyond 2.0 A resolution. Solution by molecular replacement using the E. coli amine oxidase structure [Parsons, Convery, Wilmot, Yadav, Blakeley, Corner, Philips, McPherson & Knowles (1995). Structure, 3, 1171-1184] as a search model reveals that there are three dimers in the asymmetric unit in a trigonal arrangement having 32 point-group symmetry. The solution agrees well with the self-rotation function of YAO. The non-crystallographic threefold axis lies parallel to a crystallographic twofold screw axis and each dimer has twofold symmetry. Phases from the refined model based on the molecular-replacement solution were used to solve one heavy-atom derivative. Model building from the unbiased isomorphous replacement phases is in progress.

Selected figure(s)

Figure 1.
Fig. 1. Crystals of yeast copper amine oxidase. There ae four polymorphs observed under the same crystallization conditions: (a) and (b are monoclinic crystls and (c) and (d) are orthorhombic crystals.

Figure 3.
Fig. 3. Schematic drawing of the crystallographic asymmetric unit based on the molecular­replacement solution. The asymmetric unit consists of a trigonal arrangement of dimers and has point­group symmetry D3 (32), with the local threefold axis parallel to the crystallographic a axis. The directions of the dyads in each dimer (the monomers are ditinguished by thin and thick lines) are indicated with respect to the crystallographic b and c axes.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1997, 53, 364-370) copyright 1997.

Figures were selected by an automated process.