1weh: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (15 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==Crystal structure of the conserved hypothetical protein TT1887 from Thermus thermophilus HB8== | ||
<StructureSection load='1weh' size='340' side='right'caption='[[1weh]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1weh]] is a 2 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=1WEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WEH 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]] 1.8Å</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></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=1weh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1weh OCA], [https://pdbe.org/1weh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1weh RCSB], [https://www.ebi.ac.uk/pdbsum/1weh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1weh ProSAT], [https://www.topsan.org/Proteins/RSGI/1weh TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SLJ9_THET8 Q5SLJ9_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/we/1weh_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=1weh ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
TT1887 and TT1465 from Thermus thermophilus HB8 are conserved hypothetical proteins, and are annotated as possible lysine decarboxylases in the Pfam database. Here we report the crystal structures of TT1887 and TT1465 at 1.8 A and 2.2 A resolutions, respectively, as determined by the multiwavelength anomalous dispersion (MAD) method. TT1887 is a homotetramer, while TT1465 is a homohexamer in the crystal and in solution. The structures of the TT1887 and TT1465 monomers contain single domains with the Rossmann fold, comprising six alpha helices and seven beta strands, and are quite similar to each other. The major structural differences exist in the N terminus of TT1465, where there are two additional alpha helices. A comparison of the structures revealed the elements that are responsible for the different oligomerization modes. The distributions of the electrostatic potential on the solvent-accessible surfaces suggested putative active sites. | TT1887 and TT1465 from Thermus thermophilus HB8 are conserved hypothetical proteins, and are annotated as possible lysine decarboxylases in the Pfam database. Here we report the crystal structures of TT1887 and TT1465 at 1.8 A and 2.2 A resolutions, respectively, as determined by the multiwavelength anomalous dispersion (MAD) method. TT1887 is a homotetramer, while TT1465 is a homohexamer in the crystal and in solution. The structures of the TT1887 and TT1465 monomers contain single domains with the Rossmann fold, comprising six alpha helices and seven beta strands, and are quite similar to each other. The major structural differences exist in the N terminus of TT1465, where there are two additional alpha helices. A comparison of the structures revealed the elements that are responsible for the different oligomerization modes. The distributions of the electrostatic potential on the solvent-accessible surfaces suggested putative active sites. | ||
Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8.,Kukimoto-Niino M, Murayama K, Kato-Murayama M, Idaka M, Bessho Y, Tatsuguchi A, Ushikoshi-Nakayama R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S Protein Sci. 2004 Nov;13(11):3038-42. Epub 2004 Sep 30. PMID:15459330<ref>PMID:15459330</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Idaka | <div class="pdbe-citations 1weh" style="background-color:#fffaf0;"></div> | ||
[[Category: Kukimoto-Niino | == References == | ||
[[Category: Kuramitsu | <references/> | ||
[[Category: Murayama | __TOC__ | ||
</StructureSection> | |||
[[Category: Shirouzu | [[Category: Large Structures]] | ||
[[Category: Terada | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Yokoyama | [[Category: Idaka M]] | ||
[[Category: Kukimoto-Niino M]] | |||
[[Category: Kuramitsu S]] | |||
[[Category: Murayama K]] | |||
[[Category: Shirouzu M]] | |||
[[Category: Terada T]] | |||
[[Category: Yokoyama S]] | |||
Latest revision as of 10:34, 30 October 2024
Crystal structure of the conserved hypothetical protein TT1887 from Thermus thermophilus HB8Crystal structure of the conserved hypothetical protein TT1887 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 PubMedTT1887 and TT1465 from Thermus thermophilus HB8 are conserved hypothetical proteins, and are annotated as possible lysine decarboxylases in the Pfam database. Here we report the crystal structures of TT1887 and TT1465 at 1.8 A and 2.2 A resolutions, respectively, as determined by the multiwavelength anomalous dispersion (MAD) method. TT1887 is a homotetramer, while TT1465 is a homohexamer in the crystal and in solution. The structures of the TT1887 and TT1465 monomers contain single domains with the Rossmann fold, comprising six alpha helices and seven beta strands, and are quite similar to each other. The major structural differences exist in the N terminus of TT1465, where there are two additional alpha helices. A comparison of the structures revealed the elements that are responsible for the different oligomerization modes. The distributions of the electrostatic potential on the solvent-accessible surfaces suggested putative active sites. Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8.,Kukimoto-Niino M, Murayama K, Kato-Murayama M, Idaka M, Bessho Y, Tatsuguchi A, Ushikoshi-Nakayama R, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S Protein Sci. 2004 Nov;13(11):3038-42. Epub 2004 Sep 30. PMID:15459330[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||