3ju4
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3ju4 is ON HOLD Authors: Schulz, E.C., Neuman, P., Gerardy-Schahn, R., Sheldrick, G.M., Ficner, R. Description: Crystal Structure Analysis of Endos...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==Crystal Structure Analysis of EndosialidaseNF at 0.98 A Resolution== |
| + | <StructureSection load='3ju4' size='340' side='right'caption='[[3ju4]], [[Resolution|resolution]] 0.98Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ju4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_K1F Escherichia phage K1F]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JU4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.98Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</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=3ju4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ju4 OCA], [https://pdbe.org/3ju4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ju4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ju4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ju4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FIBER_BPK1F FIBER_BPK1F] Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid.<ref>PMID:20096705</ref> <ref>PMID:3546309</ref> The C-terminal chaperone protein mediates homotrimerization and proper folding of the catalytic endo-N trimer.<ref>PMID:12556457</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/3ju4_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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=3ju4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Endosialidase NF (endoNF) is a bacteriophage-derived endosialidase that specifically degrades alpha-2,8-linked polysialic acid. The structure of a new crystal form of endoNF in complex with sialic acid has been refined at 0.98 A resolution. The 210 kDa homotrimeric multi-domain enzyme displays outstanding stability and resistance to SDS. Even at atomic resolution, only a minor fraction of side chains possess alternative conformations. However, multiple conformations of an active-site residue imply that it has an important catalytic function in the cleavage mechanism of polysialic acid. | ||
| - | + | Structure analysis of endosialidase NF at 0.98 A resolution.,Schulz EC, Neumann P, Gerardy-Schahn R, Sheldrick GM, Ficner R Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):176-80. Epub 2010 Jan 22. PMID:20124697<ref>PMID:20124697</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3ju4" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Neuraminidase 3D structures|Neuraminidase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia phage K1F]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ficner R]] | ||
| + | [[Category: Gerardy-Schahn R]] | ||
| + | [[Category: Neuman P]] | ||
| + | [[Category: Schulz EC]] | ||
| + | [[Category: Sheldrick GM]] | ||
Current revision
Crystal Structure Analysis of EndosialidaseNF at 0.98 A Resolution
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