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4n0j

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Revision as of 10:41, 11 August 2016

Crystal structure of dimethyllysine hen egg-white lysozyme in complex with sclx4 at 1.9 A resolution

Structural highlights

4n0j is a 2 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:	, , , ,
NonStd Res:	,
Related:	4ipq, 4ipr
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

Lysine is a ubiquitous residue on protein surfaces. Post translational modifications of lysine, including methylation to the mono-, di- or trimethylated amine result in chemical and structural alterations that have major consequences for protein interactions and signalling pathways. Small molecules that bind to methylated lysines are potential tools to modify such pathways. To make progress in this direction, detailed structural data of ligands in complex with methylated lysine is required. Here, we report a crystal structure of p-sulfonatocalix[4]arene (sclx4) bound to methylated lysozyme in which the lysine residues were chemically modified from Lys-NH3 + to Lys-NH(Me2)+. Of the six possible dimethyllysine sites, sclx4 selected Lys116-Me2 and the dimethylamino substituent was deeply buried in the calixarene cavity. This complex confirms the tendency for Lys-Me2 residues to form cation-pi interactions, which have been shown to be important in protein recognition of histone tails bearing methylated lysines. Supporting data from NMR spectroscopy and MD simulations confirm the selectivity for Lys116-Me2 in solution. The structure presented here may serve as a stepping stone to the development of new biochemical reagents that target methylated lysines.

Structural study of a small molecule receptor bound to dimethyllysine in lysozyme.,McGovern RE, Snarr BD, Lyons JA, McFarlane J, Whiting AL, Paci I, Hof F, Crowley PB Chem Sci. 2015 Jan 1;6(1):442-449. PMID:25530835^[2]

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

References

↑ 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
↑ McGovern RE, Snarr BD, Lyons JA, McFarlane J, Whiting AL, Paci I, Hof F, Crowley PB. Structural study of a small molecule receptor bound to dimethyllysine in lysozyme. Chem Sci. 2015 Jan 1;6(1):442-449. PMID:25530835 doi:http://dx.doi.org/10.1039/C4SC02383H

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4n0j"

Categories: Gallus gallus | Lysozyme | Crowley, P B | McGovern, R E | Hydrolase

@@ Line 1: / Line 1: @@
 ==Crystal structure of dimethyllysine hen egg-white lysozyme in complex with sclx4 at 1.9 A resolution==
 <StructureSection load='4n0j' size='340' side='right' caption='[[4n0j]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ipq|4ipq]], [[4ipr|4ipr]]</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=4n0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n0j RCSB], [http://www.ebi.ac.uk/pdbsum/4n0j PDBsum]</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=4n0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0j OCA], [http://pdbe.org/4n0j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n0j RCSB], [http://www.ebi.ac.uk/pdbsum/4n0j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0j ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4n0j" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4n0j

From Proteopedia

Revision as of 10:41, 11 August 2016

Crystal structure of dimethyllysine hen egg-white lysozyme in complex with sclx4 at 1.9 A resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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