1o7d: Difference between revisions
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[[Image:1o7d. | [[Image:1o7d.jpg|left|200px]]<br /><applet load="1o7d" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1o7d" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1o7d, resolution 2.70Å" /> | caption="1o7d, resolution 2.70Å" /> | ||
'''THE STRUCTURE OF THE BOVINE LYSOSOMAL A-MANNOSIDASE SUGGESTS A NOVEL MECHANISM FOR LOW PH ACTIVATION'''<br /> | '''THE STRUCTURE OF THE BOVINE LYSOSOMAL A-MANNOSIDASE SUGGESTS A NOVEL MECHANISM FOR LOW PH ACTIVATION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1O7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NAG, ZN, SO4 and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] | 1O7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NAG, ZN, SO4 and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] Known structural/functional Site: <scene name='pdbsite=ACT:Zn Binding Site For Chain A'>ACT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: lysosomal]] | [[Category: lysosomal]] | ||
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Revision as of 14:44, 18 December 2007
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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 Known structural/functional 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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