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==Structure of the soluble domain of the membrane protein TM1634 from Thermotoga maritima== | |||
<StructureSection load='2vko' size='340' side='right'caption='[[2vko]], [[Resolution|resolution]] 1.79Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2vko]] is a 4 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=2VKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VKO 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]] 1.79Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=2vko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vko OCA], [https://pdbe.org/2vko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vko RCSB], [https://www.ebi.ac.uk/pdbsum/2vko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vko ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9X1W9_THEMA Q9X1W9_THEMA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
As a part of the Joint Center for Structural Genomics (JCSG) biological targets, the structures of soluble domains of membrane proteins from Thermotoga maritima were pursued. Here, we report the crystal structure of the soluble domain of TM1634, a putative membrane protein of 128 residues (15.1 kDa) and unknown function. The soluble domain of TM1634 is an alpha-helical dimer that contains a single tetratrico peptide repeat (TPR) motif in each monomer where each motif is similar to that found in Tom20. The overall fold, however, is unique and a DALI search does not identify similar folds beyond the 38-residue TPR motif. Two different putative ligand binding sites, in which PEG200 and Co(2+) were located, were identified using crystallography and NMR, respectively. | |||
Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634.,McCleverty CJ, Columbus L, Kreusch A, Lesley SA Protein Sci. 2008 Mar 27;. PMID:18369189<ref>PMID:18369189</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2vko" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
= | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: | |||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: | [[Category: Columbus L]] | ||
[[Category: Kreusch A]] | |||
[[Category: Lesley SA]] | |||
[[Category: McCleverty CJ]] | |||
Latest revision as of 18:23, 13 December 2023
Structure of the soluble domain of the membrane protein TM1634 from Thermotoga maritimaStructure of the soluble domain of the membrane protein TM1634 from Thermotoga maritima
Structural highlights
FunctionPublication Abstract from PubMedAs a part of the Joint Center for Structural Genomics (JCSG) biological targets, the structures of soluble domains of membrane proteins from Thermotoga maritima were pursued. Here, we report the crystal structure of the soluble domain of TM1634, a putative membrane protein of 128 residues (15.1 kDa) and unknown function. The soluble domain of TM1634 is an alpha-helical dimer that contains a single tetratrico peptide repeat (TPR) motif in each monomer where each motif is similar to that found in Tom20. The overall fold, however, is unique and a DALI search does not identify similar folds beyond the 38-residue TPR motif. Two different putative ligand binding sites, in which PEG200 and Co(2+) were located, were identified using crystallography and NMR, respectively. Structure and ligand binding of the soluble domain of a Thermotoga maritima membrane protein of unknown function TM1634.,McCleverty CJ, Columbus L, Kreusch A, Lesley SA Protein Sci. 2008 Mar 27;. PMID:18369189[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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