3hyi
From Proteopedia
(Difference between revisions)
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<StructureSection load='3hyi' size='340' side='right'caption='[[3hyi]], [[Resolution|resolution]] 2.34Å' scene=''> | <StructureSection load='3hyi' size='340' side='right'caption='[[3hyi]], [[Resolution|resolution]] 2.34Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3hyi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3hyi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HYI FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=3hyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hyi OCA], [https://pdbe.org/3hyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hyi RCSB], [https://www.ebi.ac.uk/pdbsum/3hyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hyi 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=3hyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hyi OCA], [https://pdbe.org/3hyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hyi RCSB], [https://www.ebi.ac.uk/pdbsum/3hyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hyi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/WHIA_THEMA WHIA_THEMA] Involved in cell division and chromosome segregation.[HAMAP-Rule:MF_01420] | |
== 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=3hyi 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=3hyi ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Proteins of the DUF199 family, present in all Gram-positive bacteria and best characterized by the WhiA sporulation control factor in Streptomyces coelicolor, are thought to act as genetic regulators. The crystal structure of the DUF199/WhiA protein from Thermatoga maritima demonstrates that these proteins possess a bipartite structure, in which a degenerate N-terminal LAGLIDADG homing endonuclease (LHE) scaffold is tethered to a C-terminal helix-turn-helix (HTH) domain. The LHE domain has lost those residues critical for metal binding and catalysis, and also displays an extensively altered DNA-binding surface as compared with homing endonucleases. The HTH domain most closely resembles related regions of several bacterial sigma70 factors that bind the -35 regions of bacterial promoters. The structure illustrates how an invasive element might be transformed during evolution into a larger assemblage of protein folds that can participate in the regulation of a complex biological pathway. | ||
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| - | The structure of a bacterial DUF199/WhiA protein: domestication of an invasive endonuclease.,Kaiser BK, Clifton MC, Shen BW, Stoddard BL Structure. 2009 Oct 14;17(10):1368-76. PMID:19836336<ref>PMID:19836336</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3hyi" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 43589]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Thermotoga maritima]] |
| - | [[Category: | + | [[Category: Clifton MC]] |
| - | [[Category: | + | [[Category: Kaiser BK]] |
| - | [[Category: | + | [[Category: Shen BW]] |
| - | [[Category: | + | [[Category: Stoddard BL]] |
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Current revision
Crystal structure of full-length DUF199/WhiA from Thermatoga maritima
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