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[[Image:1hl8.gif|left|200px]]<br />
<applet load="1hl8" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hl8, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE==
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)]]
<StructureSection load='1hl8' size='340' side='right'caption='[[1hl8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HL8 OCA]].
</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>
 
<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>
==Reference==
<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>
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]
</table>
[[Category: Alpha-L-fucosidase]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/Q9WYE2_THEMA Q9WYE2_THEMA]
[[Category: Thermotoga maritima]]
== Evolutionary Conservation ==
[[Category: Bignon, C.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Bourne, Y.]]
Check<jmol>
[[Category: Henrissat, B.]]
  <jmolCheckbox>
[[Category: Sulzenbacher, G.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/1hl8_consurf.spt"</scriptWhenChecked>
[[Category: alpha-l-fucosidase]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: glycoside hydrolase]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: thermostable]]
  </jmolCheckbox>
 
</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].
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:29:30 2007''
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Bignon C]]
[[Category: Bourne Y]]
[[Category: Henrissat B]]
[[Category: Sulzenbacher G]]

Latest revision as of 14:32, 27 March 2024

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASECRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ALPHA-FUCOSIDASE

Structural highlights

1hl8 is a 2 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9WYE2_THEMA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1hl8, resolution 2.40Å

Drag the structure with the mouse to rotate

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