1hl8: Difference between revisions
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[[Image:1hl8.gif|left|200px]]<br /><applet load="1hl8" size=" | [[Image:1hl8.gif|left|200px]]<br /><applet load="1hl8" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hl8, resolution 2.40Å" /> | caption="1hl8, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE'''<br /> | '''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1HL8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Active as [http://en.wikipedia.org/wiki/Alpha-L-fucosidase Alpha-L-fucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.51 3.2.1.51] Known structural/functional Site: <scene name='pdbsite=AC1:General Acid Base, Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 1HL8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Active as [http://en.wikipedia.org/wiki/Alpha-L-fucosidase Alpha-L-fucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.51 3.2.1.51] Known structural/functional Site: <scene name='pdbsite=AC1:General+Acid+Base,+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HL8 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: thermostable]] | [[Category: thermostable]] | ||
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Revision as of 10:50, 3 February 2008
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CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE
OverviewOverview
Fucosylated glycoconjugates are involved in numerous biological events, and alpha-l-fucosidases, the enzymes responsible for their processing, are, therefore of crucial importance. Deficiency in alpha-l-fucosidase activity, is associated with fucosidosis, a lysosomal storage disorder characterized, by rapid neurodegeneration, resulting in severe mental and motor, deterioration. To gain insight into alpha-l-fucosidase function at the, molecular level, we have determined the crystal structure of Thermotoga, maritima alpha-l-fucosidase. This enzyme assembles as a hexamer and, displays a two-domain fold, composed of a catalytic (beta/alpha)(8)-like, domain and a C-terminal beta-sandwich domain. The structures of an, enzyme-product complex and of a covalent glycosyl-enzyme intermediate, coupled with kinetic and mutagenesis studies, allowed us to identify the, catalytic nucleophile, Asp(244), and the Bronsted acid/base, Glu(266)., Because T. maritima alpha-l-fucosidase occupies a unique evolutionary, position, being far more closely related to the mammalian enzymes than to, any other prokaryotic homolog, a structural model of the human enzyme was, built to document the structural consequences of the genetic mutations, associated with fucosidosis.
About this StructureAbout this Structure
1HL8 is a Single protein structure of sequence from Thermotoga maritima. Active as Alpha-L-fucosidase, with EC number 3.2.1.51 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis., Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, Bourne Y, J Biol Chem. 2004 Mar 26;279(13):13119-28. Epub 2004 Jan 8. PMID:14715651
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