1o7d

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spinqualitylabelsall models 1o7d, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE STRUCTURE OF THE BOVINE LYSOSOMAL A-MANNOSIDASE SUGGESTS A NOVEL MECHANISM FOR LOW PH ACTIVATION

Overview

Lysosomal alpha-mannosidase (LAM: EC 3.2.1.24) belongs to the, sequence-based glycoside hydrolase family 38 (GH38). Two other mammalian, GH38 members, Golgi alpha-mannosidase II (GIIAM) and cytosolic, alpha-mannosidase, are expressed in all tissues. In humans, cattle, cat, and guinea pig, lack of lysosomal alpha-mannosidase activity causes the, autosomal recessive disease alpha-mannosidosis. Here, we describe the, three-dimensional structure of bovine lysosomal alpha-mannosidase (bLAM), at 2.7A resolution and confirm the solution state dimer by electron, microscopy. We present the first structure of a mammalian GH38 enzyme that, offers indications for the signal areas for mannose phosphorylation, suggests a previously undetected mechanism of low-pH activation and, provides a template for further biochemical studies of the family 38, glycoside hydrolases as well as lysosomal transport. Furthermore, it, provides a basis for understanding the human form of alpha-mannosidosis at, the atomic level. The atomic coordinates and structure factors have been, deposited in the Protein Data Bank (accession codes 1o7d and r1o7dsf).

About this Structure

1O7D is a Single protein structure of sequence from Bos taurus with NAG, ZN, SO4 and TRS as ligands. Active as Alpha-mannosidase, with EC number 3.2.1.24 Structure known Active Site: ACT. Full crystallographic information is available from OCA.

Reference

The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation., Heikinheimo P, Helland R, Leiros HK, Leiros I, Karlsen S, Evjen G, Ravelli R, Schoehn G, Ruigrok R, Tollersrud OK, McSweeney S, Hough E, J Mol Biol. 2003 Mar 28;327(3):631-44. PMID:12634058

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