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New page: left|200px<br /><applet load="1dkk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dkk, resolution 1.9Å" /> '''BOBWHITE QUAIL LYSOZY...
 
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[[Image:1dkk.gif|left|200px]]<br /><applet load="1dkk" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dkk, resolution 1.9&Aring;" />
'''BOBWHITE QUAIL LYSOZYME WITH NITRATE'''<br />


==Overview==
==BOBWHITE QUAIL LYSOZYME WITH NITRATE==
The HyHEL-5 antibody has more than a thousandfold lower affinity for, bobwhite quail lysozyme (BWQL) than for hen egg-white lysozyme (HEL). Four, sequence differences exist between BWQL and HEL, of which only one is, involved in the interface with the Fab. The structure of bobwhite quail, lysozyme has been determined in the uncomplexed state in two different, crystal forms and in the complexed state with HyHEL-5, an antihen, egg-white lysozyme Fab. Similar backbone conformations are observed in the, three molecules of the two crystal forms of uncomplexed BWQL, although, they show considerable variability in side-chain conformation. A, relatively mobile segment in uncomplexed BWQL is observed to be part of, the HyHEL-5 epitope. No major backbone conformational differences are, observed in the lysozyme upon complex formation, but side-chain, conformational differences are seen in surface residues that are involved, in the interface with the antibody. The hydrogen bonding in the interface, between BWQL and HyHEL-5 is similar to that in previously determined, lysozyme-HyHEL-5 complexes.
<StructureSection load='1dkk' size='340' side='right'caption='[[1dkk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dkk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Colinus_virginianus Colinus virginianus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DKK 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=1dkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkk OCA], [https://pdbe.org/1dkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dkk RCSB], [https://www.ebi.ac.uk/pdbsum/1dkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dkk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSC_COLVI LYSC_COLVI] 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/dk/1dkk_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=1dkk ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1DKK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Colinus_virginianus Colinus virginianus] with NO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DKK OCA].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Refined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment., Chacko S, Silverton EW, Smith-Gill SJ, Davies DR, Shick KA, Xavier KA, Willson RC, Jeffrey PD, Chang CY, Sieker LC, Sheriff S, Proteins. 1996 Sep;26(1):55-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8880929 8880929]
[[Category: Colinus virginianus]]
[[Category: Colinus virginianus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Jeffrey PD]]
[[Category: Jeffrey, P.D.]]
[[Category: Sheriff S]]
[[Category: Sheriff, S.]]
[[Category: NO3]]
[[Category: bacteriolytic enzyme]]
[[Category: glycosidase]]
[[Category: hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:21:42 2007''

Latest revision as of 09:51, 20 March 2024

BOBWHITE QUAIL LYSOZYME WITH NITRATE

1dkk, resolution 1.90Å

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