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.


1hl8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:32, 27 March 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hl8.gif|left|200px]]
 
-
{{Structure
+
==CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE==
-
|PDB= 1hl8 |SIZE=350|CAPTION= <scene name='initialview01'>1hl8</scene>, resolution 2.40&Aring;
+
<StructureSection load='1hl8' size='340' side='right'caption='[[1hl8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=AC1:General+Acid+Base,+Chain+B'>AC1</scene>
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1hl8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HL8 FirstGlance]. <br>
-
|ACTIVITY= [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]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
-
}}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hl8 OCA], [https://pdbe.org/1hl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hl8 RCSB], [https://www.ebi.ac.uk/pdbsum/1hl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hl8 ProSAT]</span></td></tr>
-
 
+
</table>
-
'''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/Q9WYE2_THEMA Q9WYE2_THEMA]
-
 
+
== Evolutionary Conservation ==
-
==Overview==
+
[[Image:Consurf_key_small.gif|200px|right]]
-
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.
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==About this Structure==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/1hl8_consurf.spt"</scriptWhenChecked>
-
1HL8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HL8 OCA].
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
 
+
<text>to colour the structure by Evolutionary Conservation</text>
-
==Reference==
+
</jmolCheckbox>
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/14715651 14715651]
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hl8 ConSurf].
-
[[Category: Alpha-L-fucosidase]]
+
<div style="clear:both"></div>
-
[[Category: Single protein]]
+
__TOC__
-
[[Category: Thermotoga maritima]]
+
</StructureSection>
-
[[Category: Bignon, C.]]
+
[[Category: Large Structures]]
-
[[Category: Bourne, Y.]]
+
[[Category: Thermotoga maritima MSB8]]
-
[[Category: Henrissat, B.]]
+
[[Category: Bignon C]]
-
[[Category: Sulzenbacher, G.]]
+
[[Category: Bourne Y]]
-
[[Category: alpha-l-fucosidase]]
+
[[Category: Henrissat B]]
-
[[Category: glycoside hydrolase]]
+
[[Category: Sulzenbacher G]]
-
[[Category: thermostable]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:33 2008''
+

Current revision

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE

PDB ID 1hl8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hl8"
Personal tools