2f5t: Difference between revisions

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<StructureSection load='2f5t' size='340' side='right'caption='[[2f5t]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
<StructureSection load='2f5t' size='340' side='right'caption='[[2f5t]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2f5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/'caldococcus_litoralis'_z-1301 'caldococcus litoralis' z-1301]. 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>
<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]] 1.45&#8491;</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]]
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</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&reg;/PubMed&reg;, 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==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Caldococcus litoralis z-1301]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Boos, W]]
[[Category: Thermococcus litoralis]]
[[Category: Diederichs, K]]
[[Category: Boos W]]
[[Category: Krug, M]]
[[Category: Diederichs K]]
[[Category: Lee, S J]]
[[Category: Krug M]]
[[Category: Welte, W]]
[[Category: Lee SJ]]
[[Category: Sugar-binding]]
[[Category: Welte W]]
[[Category: Transcription]]
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