1sng

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[[Image:1sng.gif|left|200px]]
 
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{{Structure
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==Structure of a Thermophilic Serpin in the Native State==
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|PDB= 1sng |SIZE=350|CAPTION= <scene name='initialview01'>1sng</scene>, resolution 1.76&Aring;
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<StructureSection load='1sng' size='340' side='right'caption='[[1sng]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1sng]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SNG FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.76&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAF:S-DIMETHYLARSINOYL-CYSTEINE'>CAF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1sng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sng OCA], [https://pdbe.org/1sng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sng RCSB], [https://www.ebi.ac.uk/pdbsum/1sng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sng ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q47NK3_THEFY Q47NK3_THEFY]
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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/sn/1sng_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=1sng 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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Serpins fold into a native metastable state and utilize a complex conformational change to inhibit target proteases. An undesirable result of this conformational flexibility is that most inhibitory serpins are heat sensitive, forming inactive polymers at elevated temperatures. However, the prokaryote serpin, thermopin, from Thermobifida fusca is able to function in a heated environment. We have determined the 1.8 A x-ray crystal structure of thermopin in the native, inhibitory conformation. A structural comparison with the previously determined 1.5 A structure of cleaved thermopin provides detailed insight into the complex mechanism of conformational change in serpins. Flexibility in the shutter region and electrostatic interactions at the top of the A beta-sheet (the breach) involving the C-terminal tail, a unique structural feature of thermopin, are postulated to be important for controlling inhibitory activity and triggering conformational change, respectively, in the native state. Here we have discussed the structural basis of how this serpin reconciles the thermodynamic instability necessary for function with the stability required to withstand elevated temperatures.
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'''Structure of a Thermophilic Serpin in the Native State'''
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The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition.,Fulton KF, Buckle AM, Cabrita LD, Irving JA, Butcher RE, Smith I, Reeve S, Lesk AM, Bottomley SP, Rossjohn J, Whisstock JC J Biol Chem. 2005 Mar 4;280(9):8435-42. Epub 2004 Dec 7. PMID:15590653<ref>PMID:15590653</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1sng" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Serpins fold into a native metastable state and utilize a complex conformational change to inhibit target proteases. An undesirable result of this conformational flexibility is that most inhibitory serpins are heat sensitive, forming inactive polymers at elevated temperatures. However, the prokaryote serpin, thermopin, from Thermobifida fusca is able to function in a heated environment. We have determined the 1.8 A x-ray crystal structure of thermopin in the native, inhibitory conformation. A structural comparison with the previously determined 1.5 A structure of cleaved thermopin provides detailed insight into the complex mechanism of conformational change in serpins. Flexibility in the shutter region and electrostatic interactions at the top of the A beta-sheet (the breach) involving the C-terminal tail, a unique structural feature of thermopin, are postulated to be important for controlling inhibitory activity and triggering conformational change, respectively, in the native state. Here we have discussed the structural basis of how this serpin reconciles the thermodynamic instability necessary for function with the stability required to withstand elevated temperatures.
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*[[Serpin 3D structures|Serpin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1SNG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SNG OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition., Fulton KF, Buckle AM, Cabrita LD, Irving JA, Butcher RE, Smith I, Reeve S, Lesk AM, Bottomley SP, Rossjohn J, Whisstock JC, J Biol Chem. 2005 Mar 4;280(9):8435-42. Epub 2004 Dec 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15590653 15590653]
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[[Category: Single protein]]
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[[Category: Thermobifida fusca]]
[[Category: Thermobifida fusca]]
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[[Category: Bottomley, S P.]]
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[[Category: Bottomley SP]]
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[[Category: Buckle, A M.]]
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[[Category: Buckle AM]]
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[[Category: Butcher, R E.]]
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[[Category: Butcher RE]]
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[[Category: Cabrita, L D.]]
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[[Category: Cabrita LD]]
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[[Category: Fulton, K F.]]
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[[Category: Fulton KF]]
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[[Category: Irving, J A.]]
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[[Category: Irving JA]]
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[[Category: Lesk, A M.]]
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[[Category: Lesk AM]]
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[[Category: Reeve, S.]]
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[[Category: Reeve S]]
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[[Category: Rossjohn, J.]]
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[[Category: Rossjohn J]]
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[[Category: Smith, I.]]
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[[Category: Smith I]]
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[[Category: Whisstock, J C.]]
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[[Category: Whisstock JC]]
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[[Category: SO4]]
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[[Category: native state.]]
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[[Category: serine protease inhibitor (serpin)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:07:16 2008''
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Current revision

Structure of a Thermophilic Serpin in the Native State

PDB ID 1sng

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