2f5t
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='2f5t' size='340' side='right'caption='[[2f5t]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='2f5t' size='340' side='right'caption='[[2f5t]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2f5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2f5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_litoralis Thermococcus litoralis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F5T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=2f5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f5t OCA], [https://pdbe.org/2f5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f5t RCSB], [https://www.ebi.ac.uk/pdbsum/2f5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f5t 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=2f5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f5t OCA], [https://pdbe.org/2f5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f5t RCSB], [https://www.ebi.ac.uk/pdbsum/2f5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f5t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRMBR_THELN TRMBR_THELN] Inhibits transcription of the trehalose/maltose transport gene cluster (malE operon). Acts by binding to two different operator sequences in the promoter, preventing polymerase recruitment and transcription.<ref>PMID:12426307</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 17: | Line 20: | ||
</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=2f5t 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=2f5t ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | TrmB is an alpha-glucoside-sensing transcriptional regulator controlling two operons encoding maltose/trehalose and maltodextrin ABC transporters of Pyrococcus furiosus. The crystal structure of an N-terminal truncated derivative of TrmB (amino acids 2-109 deleted; TrmB(delta2-109)) was solved at 1.5 A resolution. This protein has lost its DNA binding domain but has retained its sugar recognition site. The structure represents a novel sugar-binding fold. TrmB(delta2-109) bound maltose, glucose, sucrose, and maltotriose, exhibiting Kd values of 6.8, 25, 34, and 160 microM, respectively. TrmB(delta2-109) behaved as a monomer in dilute buffer solution in contrast to the full-length protein, which is a dimer. Co-crystallization with bound maltose identified a binding site involving seven amino acid residues: Ser229, Asn305, Gly320, Met321, Val324, Ile325, and Glu326. Six of these residues interact with the nonreducing glucosyl residue of maltose. The nonreducing glucosyl residue is shared by all substrates bound to TrmB, suggesting it as a common recognition motif. | ||
| - | |||
| - | Crystal structure of the sugar binding domain of the archaeal transcriptional regulator TrmB.,Krug M, Lee SJ, Diederichs K, Boos W, Welte W J Biol Chem. 2006 Apr 21;281(16):10976-82. Epub 2006 Feb 10. PMID:16473881<ref>PMID:16473881</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2f5t" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 33: | Line 27: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Caldococcus litoralis z-1301]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Boos | + | [[Category: Thermococcus litoralis]] |
| - | [[Category: Diederichs | + | [[Category: Boos W]] |
| - | [[Category: Krug | + | [[Category: Diederichs K]] |
| - | [[Category: Lee | + | [[Category: Krug M]] |
| - | [[Category: Welte | + | [[Category: Lee SJ]] |
| - | + | [[Category: Welte W]] | |
| - | + | ||
Current revision
Crystal Structure of the sugar binding domain of the archaeal transcriptional regulator TrmB
| |||||||||||
