View source for 5b59


==Hen egg-white lysozyme modified with a keto-ABNO.==
<StructureSection load='5b59' size='340' side='right'caption='[[5b59]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5b59]] is a 1 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=5B59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B59 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KTO:(2~{S})-2-AZANYL-3-[(2~{R},3~{S})-2-OXIDANYL-3-[[(1~{S},5~{R})-3-OXIDANYLIDENE-9-AZABICYCLO[3.3.1]NONAN-9-YL]OXY]-1,2-DIHYDROINDOL-3-YL]PROPANAL'>KTO</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=5b59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b59 OCA], [https://pdbe.org/5b59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b59 RCSB], [https://www.ebi.ac.uk/pdbsum/5b59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b59 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 ==
Chemical modifications of native proteins can facilitate production of supernatural protein functions that are not easily accessible by complementary methods relying on genetic manipulations. However, accomplishing precise control over selectivity while maintaining structural integrity and homogeneity still represents a formidable challenge. Herein, we report a transition metal-free method for tryptophan-selective bioconjugation of proteins that is based on an organoradical and operates under ambient conditions. This method exhibits low levels of cross-reactivity and leaves higher-order structures of the protein and various functional groups therein unaffected. The strategy to target less abundant amino acids contributes to the formation of structurally homogeneous conjugates, which may even be suitable for protein crystallography. The absence of toxic metals and biochemically incompatible conditions allows a rapid functional modulation of native proteins such as antibodies and pathogenic aggregative proteins, and this method may thus easily find therapeutic applications.

Transition Metal-Free Tryptophan-Selective Bioconjugation of Proteins.,Seki Y, Ishiyama T, Sasaki D, Abe J, Sohma Y, Oisaki K, Kanai M J Am Chem Soc. 2016 Aug 31;138(34):10798-801. doi: 10.1021/jacs.6b06692. Epub, 2016 Aug 17. PMID:27534812<ref>PMID:27534812</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5b59" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Kanai M]]
[[Category: Oisaki K]]
[[Category: Sasaki D]]
[[Category: Seki Y]]
[[Category: Sohma Y]]