2d4r: Difference between revisions
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New page: left|200px<br /><applet load="2d4r" size="350" color="white" frame="true" align="right" spinBox="true" caption="2d4r, resolution 2.40Å" /> '''Crystal structure of... |
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== | ==Crystal structure of TTHA0849 from Thermus thermophilus HB8== | ||
The crystal structure of a conserved hypothetical protein, TTHA0849 from | <StructureSection load='2d4r' size='340' side='right'caption='[[2d4r]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2d4r]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D4R FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2d4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d4r OCA], [https://pdbe.org/2d4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d4r RCSB], [https://www.ebi.ac.uk/pdbsum/2d4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d4r ProSAT], [https://www.topsan.org/Proteins/RSGI/2d4r TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SK03_THET8 Q5SK03_THET8] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d4/2d4r_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2d4r ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, has been determined at 2.4 A resolution as a part of a structural and functional genomics project on T. thermophilus HB8. The main-chain folding shows a compact alpha+beta motif, forming a hydrophobic cavity in the molecule. A structural similarity search reveals that it resembles those steroidogenic acute regulatory proteins that contain the lipid-transfer (START) domain, even though TTHA0849 shows comparatively weak sequence identity to polyketide cyclases. However, the size of the ligand-binding cavity is distinctly smaller than other START domain-containing proteins, suggesting that it catalyses the transfer of smaller ligand molecules. | |||
Structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, at 2.4 A resolution: a putative member of the StAR-related lipid-transfer (START) domain superfamily.,Nakabayashi M, Shibata N, Komori H, Ueda Y, Iino H, Ebihara A, Kuramitsu S, Higuchi Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Dec 1;61(Pt, 12):1027-31. Epub 2005 Nov 5. PMID:16511226<ref>PMID:16511226</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 2d4r" style="background-color:#fffaf0;"></div> | ||
[[Category: Thermus thermophilus]] | == References == | ||
[[Category: Higuchi | <references/> | ||
[[Category: Kuramitsu | __TOC__ | ||
[[Category: Nakabayashi | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Shibata | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Higuchi Y]] | |||
[[Category: Kuramitsu S]] | |||
[[Category: Nakabayashi M]] | |||
[[Category: Shibata N]] | |||
Latest revision as of 10:50, 23 October 2024
Crystal structure of TTHA0849 from Thermus thermophilus HB8Crystal structure of TTHA0849 from Thermus thermophilus HB8
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, has been determined at 2.4 A resolution as a part of a structural and functional genomics project on T. thermophilus HB8. The main-chain folding shows a compact alpha+beta motif, forming a hydrophobic cavity in the molecule. A structural similarity search reveals that it resembles those steroidogenic acute regulatory proteins that contain the lipid-transfer (START) domain, even though TTHA0849 shows comparatively weak sequence identity to polyketide cyclases. However, the size of the ligand-binding cavity is distinctly smaller than other START domain-containing proteins, suggesting that it catalyses the transfer of smaller ligand molecules. Structure of a conserved hypothetical protein, TTHA0849 from Thermus thermophilus HB8, at 2.4 A resolution: a putative member of the StAR-related lipid-transfer (START) domain superfamily.,Nakabayashi M, Shibata N, Komori H, Ueda Y, Iino H, Ebihara A, Kuramitsu S, Higuchi Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Dec 1;61(Pt, 12):1027-31. Epub 2005 Nov 5. PMID:16511226[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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