View source for 9gyh


==HEW Lysozyme with His 15 functionalized with iodoacetamide==
<StructureSection load='9gyh' size='340' side='right'caption='[[9gyh]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9gyh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GYH 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]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1IQX:(2~{S})-2-azanyl-3-[1-(2-azanyl-2-oxidanylidene-ethyl)imidazol-4-yl]propanoic+acid'>A1IQX</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=9gyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gyh OCA], [https://pdbe.org/9gyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gyh RCSB], [https://www.ebi.ac.uk/pdbsum/9gyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gyh ProSAT]</span></td></tr>
</table>
== Function ==
[https://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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hen egg-white lysozyme (HEWL) is a small polycationic protein which is highly soluble and stable. This has led to it becoming a ;molecular laboratory' where chemical biological operations and structural techniques are tested. To date, HEWL accounts for 1233 PDB entries, roughly 0.5% of the total, making it the best-represented protein in the PDB. With the aim of unambiguously identifying the N atom of the His15 side chain that is most reactive towards iodoacetamide, the structure of chemically modified HEWL was determined by crystallizing it using the ;15 minutes lysozyme' protocol. This protocol invariably yields tetragonal crystals of the unmodified protein. To our surprise, we found that the crystals of the modified protein had similar unit-cell parameters but that refinement was only possible when considering an orthorhombic system.

The structure of His15 acetamide-modified hen egg-white lysozyme: a nice surprise from an old friend.,Malanho da Silva J, Lanuza J, Bruno F, Calderone V, Ravera E Acta Crystallogr F Struct Biol Commun. 2025 Feb 1;81(Pt 2):41-46. doi: , 10.1107/S2053230X2500010X. Epub 2025 Jan 13. PMID:39804568<ref>PMID:39804568</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9gyh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Bruno F]]
[[Category: Calderone V]]
[[Category: Delgado JML]]
[[Category: Ravera E]]
[[Category: Da Silva JSP]]