1sli

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[[Image:1sli.gif|left|200px]]
 
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==LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH DANA==
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The line below this paragraph, containing "STRUCTURE_1sli", creates the "Structure Box" on the page.
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<StructureSection load='1sli' size='340' side='right'caption='[[1sli]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1sli]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Macrobdella_decora Macrobdella decora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SLI FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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&#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=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene></td></tr>
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{{STRUCTURE_1sli| PDB=1sli | SCENE= }}
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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=1sli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sli OCA], [https://pdbe.org/1sli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sli RCSB], [https://www.ebi.ac.uk/pdbsum/1sli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sli ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NANL_MACDE NANL_MACDE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sl/1sli_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1sli ConSurf].
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<div style="clear:both"></div>
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'''LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH DANA'''
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==See Also==
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*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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BACKGROUND: Intramolecular trans-sialidase from leech (Macrobdella decora) is a unique enzyme which cleaves the terminal neuraminic acid (NeuAc) residue from sialoglycoconjugates, releasing 2, 7-anhydro-neuraminic acid (2,7-anhydro-NeuAc). It is the first enzyme found to exhibit strictly specific cleavage of NeuAc alpha2--&gt;3Gal linkages in sialoglycoconjugates. The release of 2,7-anhydro-NeuAc instead of NeuAc implies a unique mechanism, in which the sialosyl linkage is transferred within the sialoglycoconjugate rather than hydrolyzed. The aims of the structural study were to gain structural insight into the strict specificity and unique mechanism of this unusual enzyme. Results:. The 2.0 A crystal structure of recombinant leech intramolecular trans-sialidase has been solved by multiple isomorphous replacement. The 1.8 A structure of the enzyme in complex with 2-deoxy-2, 3-didehydro-NeuAc was also solved. The refined model comprising residues 81-769 has a catalytic beta-propeller domain (C), a N-terminal lectin-like domain (II) and an irregular beta-stranded domain (III) inserted into the catalytic domain. The structure reveals several possible carbohydrate-binding features: domain II has a concave face, like that of other sialidases, and there is a suitable surface charge distribution at the domain III-C interface. CONCLUSIONS: Structural comparisons showed closer evolutionary relationships to bacterial sialidases than to viral neuraminidases. Mainchain and sidechain atoms around Thr593 make the glycerol-binding pocket incapable of accommodating an extended equatorial 6-glycerol group, implying that the 6-glycerol group of the reaction intermediate may occupy an axial position, which is also required by the catalytic mechanism. The steric hindrance introduced by the bulky sidechain of Trp734 above the 2-carboxylate group may explain the lack of water involvement in the cleavage reaction and the substrate specificity.
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[[Category: Large Structures]]
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==About this Structure==
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1SLI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Macrobdella_decora Macrobdella decora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLI OCA].
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==Reference==
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The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2--&gt;3Gal specificity., Luo Y, Li SC, Chou MY, Li YT, Luo M, Structure. 1998 Apr 15;6(4):521-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9562562 9562562]
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[[Category: Exo-alpha-sialidase]]
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[[Category: Macrobdella decora]]
[[Category: Macrobdella decora]]
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[[Category: Single protein]]
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[[Category: Chou MY]]
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[[Category: Chou, M Y.]]
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[[Category: Li SC]]
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[[Category: Li, S C.]]
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[[Category: Li YT]]
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[[Category: Li, Y T.]]
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[[Category: Luo M]]
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[[Category: Luo, M.]]
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[[Category: Luo Y]]
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[[Category: Luo, Y.]]
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[[Category: Hydrolase]]
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[[Category: Intramolecular trans-sialidase]]
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[[Category: Neuraminidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:51:15 2008''
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Current revision

LEECH INTRAMOLECULAR TRANS-SIALIDASE COMPLEXED WITH DANA

PDB ID 1sli

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