3ulr
From Proteopedia
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- | [[Image:3ulr.png|left|200px]] | ||
- | + | ==Lysozyme contamination facilitates crystallization of a hetero-trimericCortactin:Arg:Lysozyme complex== | |
+ | <StructureSection load='3ulr' size='340' side='right'caption='[[3ulr]], [[Resolution|resolution]] 1.65Å' 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]] 1.65Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3ulr" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
- | *[[ | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
+ | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
- | [[Category: Boggon | + | [[Category: Boggon TJ]] |
- | [[Category: Koleske | + | [[Category: Koleske AJ]] |
- | [[Category: Liu | + | [[Category: Liu W]] |
- | [[Category: MacGrath | + | [[Category: MacGrath S]] |
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Current revision
Lysozyme contamination facilitates crystallization of a hetero-trimericCortactin:Arg:Lysozyme complex
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