View source for 2eql

==CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION==
<StructureSection load='2eql' size='340' side='right' caption='[[2eql]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2eql]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EQL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EQL FirstGlance]. <br>
</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=2eql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eql OCA], [http://pdbe.org/2eql PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eql RCSB], [http://www.ebi.ac.uk/pdbsum/2eql PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/LYSC1_HORSE LYSC1_HORSE]] 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. 
== 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/eq/2eql_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2eql ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The crystal structure of a calcium binding equine lysozyme has been determined at 2.5 A resolution by means of molecular replacement. The energy minimized equine lysozyme as the starting model, was refined with the molecular dynamics program, X-PLOR, and the R factor of the current model was found to be 24% without any water molecules. The conformation of the calcium binding loop is similar to that of alpha-lactalbumin. The profiles of backbone atomic displacements throughout the lysozyme and alpha-lactalbumin superfamilies are comparable as well as their homologous tertiary structures.

Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution.,Tsuge H, Ago H, Noma M, Nitta K, Sugai S, Miyano M J Biochem. 1992 Feb;111(2):141-3. PMID:1569037<ref>PMID:1569037</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 2eql" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Ago, H]]
[[Category: Miyano, M]]
[[Category: Tsuge, H]]