This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3ufd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:23, 1 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==C.Esp1396I bound to its highest affinity operator site OM==
==C.Esp1396I bound to its highest affinity operator site OM==
-
<StructureSection load='3ufd' size='340' side='right' caption='[[3ufd]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+
<StructureSection load='3ufd' size='340' side='right'caption='[[3ufd]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3ufd]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UFD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UFD FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3ufd]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_sp._RFL1396 Enterobacter sp. RFL1396]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UFD FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.8&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3clc|3clc]], [[3g5g|3g5g]], [[3fya|3fya]], [[3s8q|3s8q]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ufd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ufd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ufd RCSB], [http://www.ebi.ac.uk/pdbsum/3ufd PDBsum]</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=3ufd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ufd OCA], [https://pdbe.org/3ufd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ufd RCSB], [https://www.ebi.ac.uk/pdbsum/3ufd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ufd ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q8GGH0_9ENTR Q8GGH0_9ENTR]
-
Controller (C) proteins regulate the expression of restriction-modification (RM) genes in a wide variety of RM systems. However, the RM system Esp1396I is of particular interest as the C protein regulates both the restriction endonuclease (R) gene and the methyltransferase (M) gene. The mechanism of this finely tuned genetic switch depends on differential binding affinities for the promoters controlling the R and M genes, which in turn depends on differential DNA sequence recognition and the ability to recognize dual symmetries. We report here the crystal structure of the C protein bound to the M promoter, and compare the binding affinities for each operator sequence by surface plasmon resonance. Comparison of the structure of the transcriptional repression complex at the M promoter with that of the transcriptional activation complex at the R promoter shows how subtle changes in protein-DNA interactions, underpinned by small conformational changes in the protein, can explain the molecular basis of differential regulation of gene expression.
+
-
 
+
-
The structural basis of differential DNA sequence recognition by restriction-modification controller proteins.,Ball NJ, McGeehan JE, Streeter SD, Thresh SJ, Kneale GG Nucleic Acids Res. 2012 Aug 31. PMID:22941636<ref>PMID:22941636</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ball, N J]]
+
[[Category: Enterobacter sp. RFL1396]]
-
[[Category: Kneale, G G]]
+
[[Category: Large Structures]]
-
[[Category: McGeehan, J E]]
+
[[Category: Ball NJ]]
-
[[Category: Streeter, S D]]
+
[[Category: Kneale GG]]
-
[[Category: Thresh, S J]]
+
[[Category: McGeehan JE]]
-
[[Category: Bacterial gene regulatory protein]]
+
[[Category: Streeter SD]]
-
[[Category: Dna binding protein-dna complex]]
+
[[Category: Thresh S-J]]
-
[[Category: Helix-turn-helix]]
+

Current revision

C.Esp1396I bound to its highest affinity operator site OM

PDB ID 3ufd

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ufd"
Personal tools