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New page: left|200px<br /><applet load="1tlv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tlv, resolution 1.95Å" /> '''Structure of the nat...
 
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[[Image:1tlv.gif|left|200px]]<br /><applet load="1tlv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tlv, resolution 1.95&Aring;" />
'''Structure of the native and inactive LicT PRD from B. subtilis'''<br />


==Overview==
==Structure of the native and inactive LicT PRD from B. subtilis==
The transcriptional antiterminator protein LicT regulates the expression, of Bacillus subtilis operons involved in beta-glucoside metabolism. It, consists of an N-terminal RNA-binding domain (co-antiterminator (CAT)) and, two phosphorylatable phosphotransferase system regulation domains (PRD1, and PRD2). In the activated state, each PRD forms a dimeric unit with the, phosphorylation sites totally buried at the dimer interface. Here we, present the 1.95 A resolution structure of the inactive LicT PRDs as well, as the molecular solution structure of the full-length protein deduced, from small angle x-ray scattering. Comparison of native (inactive) and, mutant (constitutively active) PRD crystal structures shows massive, tertiary and quaternary rearrangements of the entire regulatory domain. In, the inactive state, a wide swing movement of PRD2 results in dimer opening, and brings the phosphorylation sites to the protein surface. This movement, is accompanied by additional structural rearrangements of both the, PRD1-PRD1 ' interface and the CAT-PRD1 linker. Small angle x-ray, scattering experiments indicate that the amplitude of the PRD2 swing might, even be wider in solution than in the crystals. Our results suggest that, PRD2 is highly mobile in the native protein, whereas it is locked upon, activation by phosphorylation.
<StructureSection load='1tlv' size='340' side='right'caption='[[1tlv]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1tlv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TLV FirstGlance]. <br>
1TLV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TLV OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tlv OCA], [https://pdbe.org/1tlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tlv RCSB], [https://www.ebi.ac.uk/pdbsum/1tlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tlv ProSAT]</span></td></tr>
Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes., Graille M, Zhou CZ, Receveur-Brechot V, Collinet B, Declerck N, van Tilbeurgh H, J Biol Chem. 2005 Apr 15;280(15):14780-9. Epub 2005 Feb 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15699035 15699035]
</table>
== Function ==
[https://www.uniprot.org/uniprot/LICT_BACSU LICT_BACSU] Mediates positive regulation of the glucanase operon (licST) by functioning as an antiterminator factor of transcription. Prevents termination at terminator lic-t.
== 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/tl/1tlv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1tlv ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Collinet, B.]]
[[Category: Collinet B]]
[[Category: Declerck, N.]]
[[Category: Declerck N]]
[[Category: Graille, M.]]
[[Category: Graille M]]
[[Category: Receveur-Brechot, V.]]
[[Category: Receveur-Brechot V]]
[[Category: Tilbeurgh, H.van.]]
[[Category: Zhou C-Z]]
[[Category: Zhou, C.Z.]]
[[Category: Van Tilbeurgh H]]
[[Category: activation mechanism]]
[[Category: conformational change]]
[[Category: crystal structure]]
[[Category: dimer structure]]
[[Category: histidine phosphorylation]]
[[Category: hpr]]
[[Category: lict]]
[[Category: phosphoenolpyruvate (pep): sugar phosphotransferase system (pts)]]
[[Category: pts regulation domains (prd)]]
[[Category: transcriptional antitermination]]
 
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Retrieved from "https://proteopedia.org/1tlv"