1lpi: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1lpi.gif|left|200px]]<br />
-<applet load="1lpi" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1lpi, resolution 2.00&Aring;" />
-'''HEW LYSOZYME: TRP...NA CATION-PI INTERACTION'''<br />
-==Overview==
+==HEW LYSOZYME: TRP...NA CATION-PI INTERACTION==
-Experimental evidence of a cation-pi interaction between a sodium cation, (Na+) and the indole ring of residue Trp123 in a structure (2.0 A) of hen, egg-white lysozyme is presented. The geometry of the metal ion-pi, interaction observed in the protein structure (distance between the, aromatic plane and the cation approximately 4 A) is consistent with, geometries observed among small molecules crystal structures and quantum, chemistry ab initio calculations. The present crystal structure of, lysozyme provides unique structural information about the geometry of, binding of cations to pi systems in proteins. It shows that the metal, ion-pi interaction within proteins is not significantly different from, similar bindings found in small molecules and that it can be modeled by, theoretical ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9828016 (full description)]]
+<StructureSection load='1lpi' size='340' side='right'caption='[[1lpi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1lpi]] 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=1LPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LPI 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=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=1lpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lpi OCA], [https://pdbe.org/1lpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lpi RCSB], [https://www.ebi.ac.uk/pdbsum/1lpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lpi 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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lp/1lpi_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lpi ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Experimental evidence of a cation-pi interaction between a sodium cation (Na+) and the indole ring of residue Trp123 in a structure (2.0 A) of hen egg-white lysozyme is presented. The geometry of the metal ion-pi interaction observed in the protein structure (distance between the aromatic plane and the cation approximately 4 A) is consistent with geometries observed among small molecules crystal structures and quantum chemistry ab initio calculations. The present crystal structure of lysozyme provides unique structural information about the geometry of binding of cations to pi systems in proteins. It shows that the metal ion-pi interaction within proteins is not significantly different from similar bindings found in small molecules and that it can be modeled by theoretical methods.
-==About this Structure==
+Cation-pi (Na+-Trp) interactions in the crystal structure of tetragonal lysozyme.,Wouters J Protein Sci. 1998 Nov;7(11):2472-5. PMID:9828016<ref>PMID:9828016</ref>
-LPI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with NA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LPI OCA]].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Cation-pi (Na+-Trp) interactions in the crystal structure of tetragonal lysozyme., Wouters J, Protein Sci. 1998 Nov;7(11):2472-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9828016 9828016]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1lpi" style="background-color:#fffaf0;"></div>
-[[Category: Wouters, J.]]
-[[Category: NA]]
-[[Category: glycosidase]]
-[[Category: hydrolase]]
-[[Category: o-glycosyl]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:35:46 2007''
+==See Also==
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Wouters J]]