1jxx

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(New page: 200px<br /><applet load="1jxx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxx, resolution 0.89&Aring;" /> '''CRAMBIN MIXED SEQUEN...)
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[[Image:1jxx.jpg|left|200px]]<br /><applet load="1jxx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jxx, resolution 0.89&Aring;" />
 
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'''CRAMBIN MIXED SEQUENCE FORM AT 200 K. PROTEIN/WATER SUBSTATES'''<br />
 
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==Overview==
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==CRAMBIN MIXED SEQUENCE FORM AT 200 K. PROTEIN/WATER SUBSTATES==
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Diverse biochemical and biophysical experiments indicate that all, proteins, regardless of size or origin, undergo a dynamic transition near, 200 K. The cause of this shift in dynamic behavior, termed a "glass, transition," and its relation to protein function are important open, questions. One explanation postulated for the transition is solidification, of correlated motions in proteins below the transition. We verified this, conjecture by showing that crambin's radius of gyration (Rg) remains, constant below approximately 180 K. We show that both atom position and, dynamics of protein and solvent are physically coupled, leading to a novel, cooperative state. This glassy state is identified by negative slopes of, the Debye-Waller (B) factor vs. temperature. It is composed of, multisubstate side chains and solvent. Based on generalization of, Adam-Gibbs' notion of a cooperatively rearranging region and decrease of, the total entropy with temperature, we calculate the slope of the, Debye-Waller factor. The results are in accord with experiment.
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<StructureSection load='1jxx' size='340' side='right'caption='[[1jxx]], [[Resolution|resolution]] 0.89&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jxx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JXX 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]] 0.89&#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=EOH:ETHANOL'>EOH</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=1jxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jxx OCA], [https://pdbe.org/1jxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jxx RCSB], [https://www.ebi.ac.uk/pdbsum/1jxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jxx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRAM_CRAAB CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known.
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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/jx/1jxx_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=1jxx 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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Diverse biochemical and biophysical experiments indicate that all proteins, regardless of size or origin, undergo a dynamic transition near 200 K. The cause of this shift in dynamic behavior, termed a "glass transition," and its relation to protein function are important open questions. One explanation postulated for the transition is solidification of correlated motions in proteins below the transition. We verified this conjecture by showing that crambin's radius of gyration (Rg) remains constant below approximately 180 K. We show that both atom position and dynamics of protein and solvent are physically coupled, leading to a novel cooperative state. This glassy state is identified by negative slopes of the Debye-Waller (B) factor vs. temperature. It is composed of multisubstate side chains and solvent. Based on generalization of Adam-Gibbs' notion of a cooperatively rearranging region and decrease of the total entropy with temperature, we calculate the slope of the Debye-Waller factor. The results are in accord with experiment.
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==About this Structure==
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On the nature of a glassy state of matter in a hydrated protein: Relation to protein function.,Teeter MM, Yamano A, Stec B, Mohanty U Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11242-7. PMID:11572978<ref>PMID:11572978</ref>
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1JXX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica] with EOH as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JXX 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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On the nature of a glassy state of matter in a hydrated protein: Relation to protein function., Teeter MM, Yamano A, Stec B, Mohanty U, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11242-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11572978 11572978]
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</div>
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<div class="pdbe-citations 1jxx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Crambe hispanica subsp. abyssinica]]
[[Category: Crambe hispanica subsp. abyssinica]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Mohanty, U.]]
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[[Category: Mohanty U]]
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[[Category: Stec, B.]]
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[[Category: Stec B]]
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[[Category: Teeter, M.M.]]
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[[Category: Teeter MM]]
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[[Category: Yamano, A.]]
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[[Category: Yamano A]]
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[[Category: EOH]]
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[[Category: function]]
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[[Category: substate]]
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[[Category: water]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:40:42 2007''
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CRAMBIN MIXED SEQUENCE FORM AT 200 K. PROTEIN/WATER SUBSTATES

PDB ID 1jxx

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