This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1hl9
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1hl9.jpg|left|200px]]<br /><applet load="1hl9" size=" | + | [[Image:1hl9.jpg|left|200px]]<br /><applet load="1hl9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hl9, resolution 2.25Å" /> | caption="1hl9, resolution 2.25Å" /> | ||
'''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH A MECHANISM BASED INHIBITOR'''<br /> | '''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH A MECHANISM BASED INHIBITOR'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HL9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with FUF as [http://en.wikipedia.org/wiki/ligand ligand]. 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:Fuf Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1HL9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=FUF:'>FUF</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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:Fuf+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HL9 OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: thermostable]] | [[Category: thermostable]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:50:09 2008'' |
Revision as of 07:50, 3 February 2008
|
CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE IN COMPLEX WITH A MECHANISM BASED INHIBITOR
Overview
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 Structure
1HL9 is a Single protein structure of sequence from Thermotoga maritima with as ligand. Active as Alpha-L-fucosidase, with EC number 3.2.1.51 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Feb 3 09:50:09 2008
