1gxx

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(New page: 200px<br /><applet load="1gxx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gxx" /> '''SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HI...)
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[[Image:1gxx.gif|left|200px]]<br /><applet load="1gxx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gxx" />
 
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'''SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE'''<br />
 
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==Overview==
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==Solution structure of lysozyme at low and high pressure==
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The "rules" governing protein structure and stability are still poorly, understood. Important clues have come from proteins that operate under, extreme conditions, because these clarify the physical constraints on, proteins. One obvious extreme is pressure, but so far little is known of, the behavior of proteins under pressure, largely for technical reasons. We, have therefore developed new methodology for calculating structure change, in solution with pressure, using NMR chemical shift changes, and we report, the change in structure of lysozyme on going from 30 bar to 2000 bar, this, being the first solution structure of a globular protein under pressure., The alpha-helical domain is compressed by approximately 1%, due to tighter, packing between helices. The interdomain region is also compressed. By, contrast, the beta-sheet domain displays very little overall compression, but undergoes more structural distortion than the alpha-domain. The, largest volume changes tend to occur close to hydrated cavities. Because, isothermal compressibility is related to volume fluctuation, this suggests, that buried water molecules play an important role in conformational, fluctuation at normal pressures, and are implicated as the nucleation, sites for structural changes leading to pressure denaturation or channel, opening.
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<StructureSection load='1gxx' size='340' side='right'caption='[[1gxx]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gxx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXX 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">Solution NMR, 1 model</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=1gxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxx OCA], [https://pdbe.org/1gxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxx RCSB], [https://www.ebi.ac.uk/pdbsum/1gxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxx ProSAT]</span></td></tr>
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</table>
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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/gx/1gxx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1gxx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The "rules" governing protein structure and stability are still poorly understood. Important clues have come from proteins that operate under extreme conditions, because these clarify the physical constraints on proteins. One obvious extreme is pressure, but so far little is known of the behavior of proteins under pressure, largely for technical reasons. We have therefore developed new methodology for calculating structure change in solution with pressure, using NMR chemical shift changes, and we report the change in structure of lysozyme on going from 30 bar to 2000 bar, this being the first solution structure of a globular protein under pressure. The alpha-helical domain is compressed by approximately 1%, due to tighter packing between helices. The interdomain region is also compressed. By contrast, the beta-sheet domain displays very little overall compression, but undergoes more structural distortion than the alpha-domain. The largest volume changes tend to occur close to hydrated cavities. Because isothermal compressibility is related to volume fluctuation, this suggests that buried water molecules play an important role in conformational fluctuation at normal pressures, and are implicated as the nucleation sites for structural changes leading to pressure denaturation or channel opening.
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==About this Structure==
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Pressure-dependent changes in the solution structure of hen egg-white lysozyme.,Refaee M, Tezuka T, Akasaka K, Williamson MP J Mol Biol. 2003 Apr 4;327(4):857-65. PMID:12654268<ref>PMID:12654268</ref>
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1GXX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. 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=1GXX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Pressure-dependent changes in the solution structure of hen egg-white lysozyme., Refaee M, Tezuka T, Akasaka K, Williamson MP, J Mol Biol. 2003 Apr 4;327(4):857-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12654268 12654268]
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</div>
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[[Category: Gallus gallus]]
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<div class="pdbe-citations 1gxx" style="background-color:#fffaf0;"></div>
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Akasaka, K.]]
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[[Category: Refaee, M.]]
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[[Category: Williamson, M.]]
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[[Category: allergen]]
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[[Category: bacteriolytic enzyme]]
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[[Category: egg-white]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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[[Category: saccharide degradation]]
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[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:20:24 2007''
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: Akasaka K]]
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[[Category: Refaee M]]
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[[Category: Williamson M]]

Current revision

Solution structure of lysozyme at low and high pressure

PDB ID 1gxx

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