5b07

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m (Protected "5b07" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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==Lysozyme (denatured by DCl and refolded)==
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<StructureSection load='5b07' size='340' side='right' caption='[[5b07]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5b07]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B07 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b05|5b05]], [[5b06|5b06]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5b07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b07 OCA], [http://pdbe.org/5b07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b07 RCSB], [http://www.ebi.ac.uk/pdbsum/5b07 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A method of hydrogen/deuterium (H/D) exchange with an unfolding-refolding process has been applied to hen egg-white lysozyme (HWL), and accurate evaluation of its deuteration was carried out by time-of-flight mass spectroscopy. Neutron crystallography requires a suitable crystal with enough deuterium exchanged in the protein to decrease incoherent scattering from hydrogens. It is very expensive to prepare a fully deuterated protein, and therefore a simple H/D exchange technique is desirable for this purpose. Acid or base addition to protein solutions with heating effectively increased the number of deuterium up to more than 20 % of that of all hydrogen atoms, and refolded structures were determined by X-ray structure analysis at 1.8 A resolution. Refolded HWL had increased deuterium content in its protein core and its native structure, determined at atomic resolution, was fully preserved.
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The entry 5b07 is ON HOLD
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An Effective Deuterium Exchange Method for Neutron Crystal Structure Analysis with Unfolding-Refolding Processes.,Kita A, Morimoto Y Mol Biotechnol. 2015 Dec 31. PMID:26718545<ref>PMID:26718545</ref>
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Authors: Kita, A., Morimoto, Y.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Lysozyme (denatured by DCl and refolded)
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<div class="pdbe-citations 5b07" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gallus gallus]]
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[[Category: Lysozyme]]
[[Category: Kita, A]]
[[Category: Kita, A]]
[[Category: Morimoto, Y]]
[[Category: Morimoto, Y]]
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[[Category: Hydrolase]]
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[[Category: Refolded]]

Revision as of 20:07, 13 January 2016

Lysozyme (denatured by DCl and refolded)

5b07, resolution 1.80Å

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