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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation.

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).[1]

References

  1. The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation. Heikinheimo, P., Helland, R., Leiros, H.K., Leiros, I., Karlsen, S., Evjen, G., Ravelli, R., Schoehn, G., Ruigrok, R., Tollersrud, O.K., McSweeney, S., Hough, E. J. Mol. Biol. (2003) [Pubmed]
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