2b5a

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Current revision (09:16, 14 February 2024) (edit) (undo)
 
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<StructureSection load='2b5a' size='340' side='right'caption='[[2b5a]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
<StructureSection load='2b5a' size='340' side='right'caption='[[2b5a]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2b5a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/'bacillus_caldolyticus' 'bacillus caldolyticus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5A FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2b5a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_caldolyticus Bacillus caldolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
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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]] 1.543&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bclIC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1394 'Bacillus caldolyticus'])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</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=2b5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5a OCA], [https://pdbe.org/2b5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5a RCSB], [https://www.ebi.ac.uk/pdbsum/2b5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5a 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=2b5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5a OCA], [https://pdbe.org/2b5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5a RCSB], [https://www.ebi.ac.uk/pdbsum/2b5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5a ProSAT]</span></td></tr>
</table>
</table>
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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=2b5a 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=2b5a ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Protection from DNA invasion is afforded by restriction-modification systems in many bacteria. The efficiency of protection depends crucially on the relative expression levels of restriction versus methytransferase genes. This regulation is provided by a controller protein, named C protein. Studies of the Bcll system in E. coli suggest that C.Bcll functions as a negative regulator for M.Bcll expression, implying that it plays a role in defense against foreign DNA during virus infection. C.Bcll binds (Kd = 14.3 nM) to a 2-fold symmetric C box DNA sequence that overlaps with the putative -35 promoter region upstream of the bcllM and bcllC genes. The C.Bcll fold comprises five alpha helices: two helices form a helix-turn-helix motif, and the remaining three helices form the extensive dimer interface. The C.Bcll-DNA model proposed suggests that DNA bending might play an important role in gene regulation, and that Glu27 and Asp31 in C.Bcll might function critically in the regulation.
 
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Crystal structure of the restriction-modification system control element C.Bcll and mapping of its binding site.,Sawaya MR, Zhu Z, Mersha F, Chan SH, Dabur R, Xu SY, Balendiran GK Structure. 2005 Dec;13(12):1837-47. PMID:16338412<ref>PMID:16338412</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2b5a" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus caldolyticus]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Balendiran, G K]]
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[[Category: Balendiran GK]]
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[[Category: Chan, S H]]
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[[Category: Chan SH]]
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[[Category: Dabur, R]]
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[[Category: Dabur R]]
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[[Category: Mersha, F]]
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[[Category: Mersha F]]
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[[Category: Sawaya, M R]]
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[[Category: Sawaya MR]]
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[[Category: Xu, S Y]]
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[[Category: Xu SY]]
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[[Category: Zhu, Z]]
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[[Category: Zhu Z]]
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[[Category: Gene regulation]]
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[[Category: Helix-turn-helix motif]]
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Current revision

C.BclI, Control Element of the BclI Restriction-Modification System

PDB ID 2b5a

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