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1qqy

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(New page: 200px<br /><applet load="1qqy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqy, resolution 1.85&Aring;" /> '''X-RAY CRYSTAL STRUCT...)
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[[Image:1qqy.gif|left|200px]]<br /><applet load="1qqy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qqy, resolution 1.85&Aring;" />
 
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'''X-RAY CRYSTAL STRUCTURE ANALYSIS OF CANINE MILK LYSOZYME (APO-TYPE)'''<br />
 
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==Overview==
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==X-RAY CRYSTAL STRUCTURE ANALYSIS OF CANINE MILK LYSOZYME (APO-TYPE)==
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Here, we show that an unfolded intermediate of canine milk lysozyme is, extraordinarily stable compared with that of the other members of the, lysozyme-alpha-lactalbumin superfamily, which has been studied previously., The stability of the intermediate of this protein was investigated using, calorimetry, CD spectroscopy, and NMR spectroscopy, and the results were, interpreted in terms of the structure revealed by X-ray crystallography at, a resolution of 1.85 A to an R-factor of 17.8%. On the basis of the, results of the thermal unfolding, this protein unfolds in two clear, cooperative stages, and the melting temperature from the intermediate to, the unfolded states is about 20 degrees C higher than that of equine milk, lysozyme. Furthermore, the (1)H NMR spectra of canine milk lysozyme at 60, degrees C, essentially 100% of which exists in the intermediate, showed, that small resonance peaks that arise from ring-current shifts of, aliphatic protons are still present in the upfield region from 0 to -1, ppm. The protein at this temperature (60 degrees C) and pH 4.5 has been, found to bind 1-anilino-naphthalene-8-sulfonate (ANS) with enhancement of, the fluorescence intensity compared with that of native and thermally, unfolded states. We interpret that the extraordinarily stable intermediate, is a molten globule state, and the extraordinary stabilization of the, molten globule state comes from stronger protection around the C- and, D-helix of the aromatic cluster region due to the His-21 residue. The, conclusion helps to explain how the molten globule state acquires its, structure and stability.
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<StructureSection load='1qqy' size='340' side='right'caption='[[1qqy]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qqy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QQY 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]] 1.85&#8491;</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=1qqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qqy OCA], [https://pdbe.org/1qqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qqy RCSB], [https://www.ebi.ac.uk/pdbsum/1qqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qqy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC1_CANLF LYSC1_CANLF] 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.[PROSITE-ProRule:PRU00680]
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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/qq/1qqy_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=1qqy 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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1QQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. 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=1QQY OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme., Koshiba T, Yao M, Kobashigawa Y, Demura M, Nakagawa A, Tanaka I, Kuwajima K, Nitta K, Biochemistry. 2000 Mar 28;39(12):3248-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10727216 10727216]
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[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
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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: Koshiba T]]
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[[Category: Koshiba, T.]]
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[[Category: Nitta K]]
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[[Category: Nitta, K.]]
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[[Category: Tanaka I]]
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[[Category: Tanaka, I.]]
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[[Category: Yao M]]
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[[Category: Yao, M.]]
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[[Category: apo-type protein]]
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[[Category: calcium binding lysozyme]]
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[[Category: enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:54:23 2007''
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Current revision

X-RAY CRYSTAL STRUCTURE ANALYSIS OF CANINE MILK LYSOZYME (APO-TYPE)

PDB ID 1qqy

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