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1qtk

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(New page: 200px<br /><applet load="1qtk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qtk, resolution 2.03&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1qtk.gif|left|200px]]<br /><applet load="1qtk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qtk, resolution 2.03&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF KRYPTON (55 BAR)'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF KRYPTON (55 BAR)==
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X-ray diffraction is used to study the binding of xenon and krypton to a, variety of crystallised proteins: porcine pancreatic elastase; subtilisin, Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani;, collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide, dehydrogenase domain from the outer membrane protein P64k from Neisseria, meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal, delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding, domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas, pressures ranging from 8 to 20 bar, xenon is able to bind to discrete, sites in hydrophobic cavities, ligand and substrate binding pockets, and, into the pore of channel-like structures. These xenon complexes can be, used to map hydrophobic sites in proteins, or as heavy-atom derivatives in, the isomorphous replacement method of structure determination.
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<StructureSection load='1qtk' size='340' side='right'caption='[[1qtk]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qtk]] 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=1QTK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QTK FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KR:KRYPTON'>KR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qtk OCA], [https://pdbe.org/1qtk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qtk RCSB], [https://www.ebi.ac.uk/pdbsum/1qtk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qtk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qt/1qtk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1qtk ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1QTK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with NA, CL and KR as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1QTK OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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Exploring hydrophobic sites in proteins with xenon or krypton., Prange T, Schiltz M, Pernot L, Colloc'h N, Longhi S, Bourguet W, Fourme R, Proteins. 1998 Jan;30(1):61-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9443341 9443341]
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__TOC__
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</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bourguet W]]
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[[Category: Bourguet, W.]]
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[[Category: Colloc'h N]]
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[[Category: Fourme, R.]]
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[[Category: Fourme R]]
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[[Category: Longhi, S.]]
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[[Category: Longhi S]]
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[[Category: Pernot, L.]]
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[[Category: Pernot L]]
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[[Category: Prange, T.]]
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[[Category: Prange T]]
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[[Category: Schiltz, M.]]
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[[Category: Schiltz M]]
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[[Category: h, N.Colloc.]]
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[[Category: CL]]
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[[Category: KR]]
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[[Category: NA]]
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[[Category: hydrophobic cavity]]
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[[Category: krypton complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:58:24 2007''
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Current revision

CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF KRYPTON (55 BAR)

PDB ID 1qtk

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