2f5g

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Current revision (13:50, 13 March 2024) (edit) (undo)
 
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<StructureSection load='2f5g' size='340' side='right'caption='[[2f5g]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2f5g' size='340' side='right'caption='[[2f5g]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2f5g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F5G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2f5g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F5G FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2f4f|2f4f]]</div></td></tr>
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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]] 1.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f5g OCA], [https://pdbe.org/2f5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f5g RCSB], [https://www.ebi.ac.uk/pdbsum/2f5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f5g ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f5g OCA], [https://pdbe.org/2f5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f5g RCSB], [https://www.ebi.ac.uk/pdbsum/2f5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f5g ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q97Y68_SACS2 Q97Y68_SACS2]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2f5g ConSurf].
</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=2f5g ConSurf].
<div style="clear:both"></div>
<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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IS200 transposases, present in many bacteria and Archaea, appear to be distinct from other groups of transposases. To provide a structural basis for understanding the action of IS200 transposases, we have determined the crystal structure of the SSO1474 protein from Sulfolobus solfataricus, a member of the IS200 family, in both Mn(2+)-bound and Mn(2+)-free forms. Its monomer fold is distinct from other classes of structurally characterized transposases. Two monomers form a tight dimer by exchanging the C-terminal alpha-helix and by merging the two central beta-sheets into a large beta-sheet. Glu(55), His(62), and four water molecules provide the direct coordination sphere of the catalytically essential metal ion in the Mn(2+)-bound structure. His(16), Asp(59), and His(60) also play important roles in maintaining the metal binding site. The catalytic site is formed at the interface between monomers. The candidate nucleophile in the transposition mechanism, strictly conserved Tyr(121) coming from the other monomer, is turned away from the active site, suggesting that a conformational change is likely to occur during the catalytic cycle.
 
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Crystal structure of a metal ion-bound IS200 transposase.,Lee HH, Yoon JY, Kim HS, Kang JY, Kim KH, Kim DJ, Ha JY, Mikami B, Yoon HJ, Suh SW J Biol Chem. 2006 Feb 17;281(7):4261-6. Epub 2005 Dec 11. PMID:16340015<ref>PMID:16340015</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 2f5g" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Saccharolobus solfataricus]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kang, J Y]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Kim, D J]]
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[[Category: Kang JY]]
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[[Category: Kim, H S]]
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[[Category: Kim DJ]]
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[[Category: Kim, K H]]
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[[Category: Kim HS]]
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[[Category: Lee, H H]]
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[[Category: Kim KH]]
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[[Category: Suh, S W]]
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[[Category: Lee HH]]
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[[Category: Yoon, J Y]]
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[[Category: Suh SW]]
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[[Category: Dimer]]
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[[Category: Yoon JY]]
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[[Category: Gene regulation]]
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[[Category: Stem-loop binding]]
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Current revision

Crystal structure of IS200 transposase

PDB ID 2f5g

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