1TU5

Crystal structure of bovine plasma copper-containing amine oxidase

Summary for 1TU5

• Entry DOI: 10.2210/pdb1tu5/pdb
• Related: 1KSI 1N9E 1OAC
• Related PRD ID: PRD_900017
• Descriptor: Copper amine oxidase, liver isozyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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, oxidoreductase, quinoenzyme, tpq
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted, extracellular space: Q29437
• Total number of polymer chains: 2
• Total formula weight: 168216.18

Authors

Lunelli, M.,Di Paolo, M.L.,Biadene, M.,Calderone, V.,Scarpa, M.,Battistutta, R.,Rigo, A.,Zanotti, G. (deposition date: 2004-06-24, release date: 2005-02-22, Last modification date: 2023-10-25)

Primary citation

Lunelli, M.,Di Paolo, M.L.,Biadene, M.,Calderone, V.,Battistutta, R.,Scarpa, M.,Rigo, A.,Zanotti, G.
Crystal structure of amine oxidase from bovine serum.
J.Mol.Biol., 346:991-1004, 2005

PubMed Abstract: Copper-containing amine oxidase extracted from bovine serum (BSAO) was crystallized and its three-dimensional structure at 2.37A resolution is described. The biological unit of BSAO is a homodimer, formed by two monomers related to each other by a non-crystallographic 2-fold axis. Each monomer is composed of three domains, similar to those of other amine oxidases from lower species. The two monomers are structurally equivalent, despite some minor differences at the two active sites. A large funnel allows access of substrates to the active-site; another cavity, accessible to the solvent, is also present between the two monomers; this second cavity could allow the entrance of molecular oxygen necessary for the oxidative reaction. Some sugar residues, bound to Asn, were still present and visible in the electron density map, in spite of the exhaustive deglycosylation necessary to grow the crystals. The comparison of the BSAO structure with those of other resolved AO structures shows strong dissimilarities in the architecture and charge distribution of the cavities leading to the active-site, possibly explaining the differences in substrate specificity.

PubMed: 15701511
DOI: 10.1016/j.jmb.2004.12.038

Experimental method

X-RAY DIFFRACTION (2.37 Å)