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1hl8

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(New page: 200px<br /> <applet load="1hl8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hl8, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1hl8.gif|left|200px]]<br />
 
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<applet load="1hl8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hl8, resolution 2.40&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE==
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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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?14715651 (full description)]]
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<StructureSection load='1hl8' size='340' side='right'caption='[[1hl8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.51 3.2.1.51]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HL8 OCA]].
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</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>
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<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>
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==Reference==
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<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>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14715651 14715651]
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</table>
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[[Category: Single protein]]
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== Function ==
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[[Category: Thermotoga maritima]]
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[https://www.uniprot.org/uniprot/Q9WYE2_THEMA Q9WYE2_THEMA]
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[[Category: Bignon, C.]]
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== Evolutionary Conservation ==
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[[Category: Bourne, Y.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Henrissat, B.]]
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Check<jmol>
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[[Category: Sulzenbacher, G.]]
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<jmolCheckbox>
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[[Category: alpha-l-fucosidase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/1hl8_consurf.spt"</scriptWhenChecked>
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[[Category: glycoside hydrolase]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: thermostable]]
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 22:05:21 2007''
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</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].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermotoga maritima MSB8]]
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[[Category: Bignon C]]
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[[Category: Bourne Y]]
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[[Category: Henrissat B]]
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[[Category: Sulzenbacher G]]

Current revision

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE

PDB ID 1hl8

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