View source for 3ulr


==Lysozyme contamination facilitates crystallization of a hetero-trimericCortactin:Arg:Lysozyme complex==
<StructureSection load='3ulr' size='340' side='right'caption='[[3ulr]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ulr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ULR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ULR 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]] 1.65&#8491;</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=3ulr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ulr OCA], [https://pdbe.org/3ulr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ulr RCSB], [https://www.ebi.ac.uk/pdbsum/3ulr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ulr 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 ==
Crystallization of contaminating proteins is a frequently encountered problem for macromolecular crystallographers. In this study, an attempt was made to obtain a binary cocrystal structure of the SH3 domain of cortactin and a 17-residue peptide from the Arg nonreceptor tyrosine kinase encompassing a PxxPxxPxxP (PxxP1) motif. However, cocrystals could only be obtained in the presence of trace amounts of a contaminating protein. A structure solution obtained by molecular replacement followed by ARP/wARP automatic model building allowed a `sequence-by-crystallography' approach to discover that the contaminating protein was lysozyme. This 1.65 A resolution crystal structure determination of a 1:1:1 heterotrimeric complex of Arg, cortactin and lysozyme thus provides an unusual `caveat emptor' warning of the dangers that underpurified proteins harbor for macromolecular crystallographers.

Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex.,Liu W, Macgrath SM, Koleske AJ, Boggon TJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt, 2):154-8. Epub 2012 Jan 25. PMID:22297987<ref>PMID:22297987</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3ulr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Boggon TJ]]
[[Category: Koleske AJ]]
[[Category: Liu W]]
[[Category: MacGrath S]]