1v3r: Difference between revisions
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<StructureSection load='1v3r' size='340' side='right'caption='[[1v3r]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1v3r' size='340' side='right'caption='[[1v3r]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1v3r]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1v3r]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V3R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V3R FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v3s|1v3s]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1v3s|1v3s]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v3r OCA], [https://pdbe.org/1v3r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v3r RCSB], [https://www.ebi.ac.uk/pdbsum/1v3r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v3r ProSAT], [https://www.topsan.org/Proteins/RSGI/1v3r TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == |
Revision as of 09:24, 6 October 2021
Crystal structure of TT1020 from Thermus thermophilus HB8Crystal structure of TT1020 from Thermus thermophilus HB8
Structural highlights
Evolutionary 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 Thermus thermophilus HB8 genome encodes a signal transducing PII protein, GlnK. The crystal structures of GlnK have been determined in two different space groups, P2(1)2(1)2(1) and P3(1)21. The PII protein has the T-loop, which is essential for interactions with receptor proteins. In both crystal forms, three GlnK molecules form a trimer in the asymmetric unit. In one P2(1)2(1)2(1) crystal form, the three T-loops in the trimer are disordered, while in another P2(1)2(1)2(1) crystal form, the T-loop from one molecule in the trimer is ordered. In the P3(1)21 crystal, one T-loop is ordered while the other two T-loops are disordered. The conformations of the ordered T-loops significantly differ between the two crystal forms; one makes the alpha-helix in the middle of the T-loop, while the other has an extension of the beta-hairpin. Two different conformations are captured by the crystal contacts. The observation of multiple T-loop conformations suggests that the T-loop could potentially exhibit "polysterism," which would be important for interactions with receptor proteins. The crystal structures of the nucleotide-bound forms, GlnK.ATP and GlnK.ADP, have also been determined. ATP/ADP binding within a cleft at the interface of two adjacent T. thermophilus GlnK monomers might affect the conformation of the T-loop. Crystal structures of the signal transducing protein GlnK from Thermus thermophilus HB8.,Sakai H, Wang H, Takemoto-Hori C, Kaminishi T, Yamaguchi H, Kamewari Y, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S J Struct Biol. 2005 Jan;149(1):99-110. PMID:15629661[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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