1tlv

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[[Image:1tlv.gif|left|200px]]
 
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{{Structure
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==Structure of the native and inactive LicT PRD from B. subtilis==
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|PDB= 1tlv |SIZE=350|CAPTION= <scene name='initialview01'>1tlv</scene>, resolution 1.95&Aring;
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<StructureSection load='1tlv' size='340' side='right'caption='[[1tlv]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>
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<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>
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|ACTIVITY=
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</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>
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|GENE= LICT, N15A, BSU39080 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=[[1h99|1H99]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tlv OCA], [http://www.ebi.ac.uk/pdbsum/1tlv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tlv RCSB]</span>
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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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'''Structure of the native and inactive LicT PRD from B. subtilis'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tl/1tlv_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1TLV is a [[Single protein]] structure of sequence from [http://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].
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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=1tlv ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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://www.ncbi.nlm.nih.gov/pubmed/15699035 15699035]
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Collinet, B.]]
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[[Category: Collinet B]]
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[[Category: Declerck, N.]]
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[[Category: Declerck N]]
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[[Category: Graille, M.]]
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[[Category: Graille M]]
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[[Category: Receveur-Brechot, V.]]
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[[Category: Receveur-Brechot V]]
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[[Category: Tilbeurgh, H van.]]
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[[Category: Zhou C-Z]]
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[[Category: Zhou, C Z.]]
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[[Category: Van Tilbeurgh H]]
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[[Category: activation mechanism]]
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[[Category: conformational change]]
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[[Category: crystal structure]]
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[[Category: dimer structure]]
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[[Category: histidine phosphorylation]]
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[[Category: hpr]]
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[[Category: lict]]
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[[Category: phosphoenolpyruvate (pep): sugar phosphotransferase system (pts)]]
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[[Category: pts regulation domains (prd)]]
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[[Category: transcriptional antitermination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:57:55 2008''
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Current revision

Structure of the native and inactive LicT PRD from B. subtilis

PDB ID 1tlv

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OCA

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