1b37
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(New page: 200px<br /><applet load="1b37" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b37, resolution 1.9Å" /> '''A 30 ANGSTROM U-SHAPE...)
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Revision as of 09:12, 20 November 2007
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A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE
Overview
BACKGROUND: Polyamines are essential for cell growth and differentiation;, compounds interfering with their metabolism are potential anticancer, agents. Polyamine oxidase (PAO) plays a central role in polyamine, homeostasis. The enzyme utilises an FAD cofactor to catalyse the oxidation, of the secondary amino groups of spermine and spermidine. RESULTS: The, first crystal structure of a polyamine oxidase has been determined to a, resolution of 1.9 Angstroms. PAO from Zea mays contains two domains, which, define a remarkable 30 Angstrom long U-shaped catalytic tunnel at their, interface. The structure of PAO in complex with the inhibitor MDL72527, reveals the residues forming the catalytic machinery and unusual, enzyme-inhibitor CH.O H bonds. A ring of glutamate and aspartate residues, surrounding one of the two tunnel openings contributes to the steering of, the substrate towards the inside of the tunnel. CONCLUSIONS: PAO, specifically oxidizes substrates that have both primary and secondary, amino groups. The complex with MDL72527 shows that the primary amino, groups are essential for the proper alignment of the substrate with, respect to the flavin. Conservation of an N-terminal sequence motif, indicates that PAO is member of a novel family of flavoenzymes. Among, these, monoamine oxidase displays significant sequence homology with PAO, suggesting a similar overall folding topology.
About this Structure
1B37 is a Single protein structure of sequence from Zea mays with NAG and FAD as ligands. Active as Polyamine oxidase, with EC number 1.5.3.11 Full crystallographic information is available from OCA.
Reference
A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase., Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A, Structure. 1999 Mar 15;7(3):265-76. PMID:10368296
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