5f14: Difference between revisions

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==Structure of native hen egg-white lysozyme==
==Structure of native hen egg-white lysozyme==
<StructureSection load='5f14' size='340' side='right' caption='[[5f14]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='5f14' size='340' side='right'caption='[[5f14]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5f14]] 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=5F14 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F14 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5f14]] 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=5F14 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F14 FirstGlance]. <br>
</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=NA:SODIUM+ION'>NA</scene></td></tr>
</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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iee|1iee]], [[5f16|5f16]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iee|1iee]], [[5f16|5f16]]</td></tr>
<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>
<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>
<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=5f14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f14 OCA], [http://pdbe.org/5f14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f14 RCSB], [http://www.ebi.ac.uk/pdbsum/5f14 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5f14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f14 OCA], [http://pdbe.org/5f14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f14 RCSB], [http://www.ebi.ac.uk/pdbsum/5f14 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f14 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</div>
</div>
<div class="pdbe-citations 5f14" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5f14" style="background-color:#fffaf0;"></div>
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: McGlone, C]]
[[Category: McGlone, C]]

Revision as of 10:54, 29 April 2020

Structure of native hen egg-white lysozymeStructure of native hen egg-white lysozyme

Structural highlights

5f14 is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Lysozyme, with EC number 3.2.1.17
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1]

Publication Abstract from PubMed

Polymers are often conjugated to proteins to improve stability; however, the impact of polymer chain length and functional groups on protein structure and function is not well understood. Here, we use RAFT polymerization to grow polymers of different lengths and functionality from a short acrylamide oligomer with a RAFT end group conjugated to lysozyme. We show by X-ray crystallography that enzyme structure is minimally impacted by modification with the RAFT end group. Significant activity toward the negatively charged Micrococcus lysodeicticus cell wall was maintained when lysozyme was modified with cationic polymers. Thermal and chemical stability of the conjugates were characterized using differential scanning fluorimetry and tryptophan fluorescence. All conjugates had a lower melting temperature; however, conjugates containing ionic or substrate mimicking polymers were more resistant to denaturation by guanidine hydrochloride. Our results demonstrate that tailoring polymer functionality can improve conjugate activity and minimize enzymatic inactivation by denaturants.

Investigating the Impact of Polymer Functional Groups on the Stability and Activity of Lysozyme-Polymer Conjugates.,Lucius M, Falatach R, McGlone C, Makaroff K, Danielson AP, Williams C, Nix JC, Konkolewicz D, Page RC, Berberich JA Biomacromolecules. 2016 Feb 11. PMID:26866284[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. Lucius M, Falatach R, McGlone C, Makaroff K, Danielson AP, Williams C, Nix JC, Konkolewicz D, Page RC, Berberich JA. Investigating the Impact of Polymer Functional Groups on the Stability and Activity of Lysozyme-Polymer Conjugates. Biomacromolecules. 2016 Feb 11. PMID:26866284 doi:http://dx.doi.org/10.1021/acs.biomac.5b01743

5f14, resolution 1.15Å

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