1N9E

Crystal structure of Pichia pastoris Lysyl Oxidase PPLO

Summary for 1N9E

• Entry DOI: 10.2210/pdb1n9e/pdb
• Related: 1A2V 1AV4 1KSI 1OAC
• Descriptor: LYSYL OXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: amine oxidase, quinoprotein, topaquinone enzyme, tpq, oxidoreductase
• Biological source: Pichia pastoris
• Total number of polymer chains: 4
• Total formula weight: 367704.00

Authors

Guss, J.M.,Duff, A.P. (deposition date: 2002-11-24, release date: 2004-01-13, Last modification date: 2023-10-25)

Primary citation

Duff, A.P.,Cohen, A.E.,Ellis, P.J.,Kuchar, J.A.,Langley, D.B.,Shepard, E.M.,Dooley, D.M.,Freeman, H.C.,Guss, J.M.
The Crystal Structure of Pichia pastoris Lysyl Oxidase
Biochemistry, 42:15148-15157, 2003

PubMed Abstract: Pichia pastoris lysyl oxidase (PPLO) is unique among the structurally characterized copper amine oxidases in being able to oxidize the side chain of lysine residues in polypeptides. Remarkably, the yeast PPLO is nearly as effective in oxidizing a mammalian tropoelastin substrate as is a true mammalian lysyl oxidase isolated from bovine aorta. Thus, PPLO is functionally related to the copper-containing lysyl oxidases despite the lack of any significant sequence similarity with these enzymes. The structure of PPLO has been determined at 1.65 A resolution. PPLO is a homodimer in which each subunit contains a Type II copper atom and a topaquinone cofactor (TPQ) formed by the posttranslational modification of a tyrosine residue. While PPLO has tertiary and quaternary topologies similar to those found in other quinone-containing copper amine oxidases, its active site is substantially more exposed and accessible. The structural elements that are responsible for the accessibility of the active site are identified and discussed.

PubMed: 14690425
DOI: 10.1021/bi035338v

Experimental method

X-RAY DIFFRACTION (1.65 Å)