2f7c

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[[Image:2f7c.jpg|left|200px]]
 
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==CatM effector binding domain with its effector cis,cis-muconate==
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The line below this paragraph, containing "STRUCTURE_2f7c", creates the "Structure Box" on the page.
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<StructureSection load='2f7c' size='340' side='right'caption='[[2f7c]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2f7c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi Acinetobacter baylyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F7C FirstGlance]. <br>
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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]] 2.162&#8491;</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=CCU:(2Z,4Z)-HEXA-2,4-DIENEDIOIC+ACID'>CCU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2f7c| PDB=2f7c | SCENE= }}
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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=2f7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7c OCA], [https://pdbe.org/2f7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f7c RCSB], [https://www.ebi.ac.uk/pdbsum/2f7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f7c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CATM_ACIAD CATM_ACIAD] Positively regulates the expression of catA, catBCIJFD and benPK in response to cis,cis-muconate. It binds to the catB-catM intercistronic region, to a specific sequence upstream of catA and to the benPK promoter region. Can also repress pca genes.<ref>PMID:7592340</ref> <ref>PMID:11932465</ref> <ref>PMID:12620848</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<text>to colour the structure by Evolutionary Conservation</text>
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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=2f7c ConSurf].
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<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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BenM, a bacterial transcriptional regulator, responds synergistically to two effectors, benzoate and cis,cis-muconate. CatM, a paralog with overlapping function, responds only to muconate. Structures of their effector-binding domains revealed two effector-binding sites in BenM. BenM and CatM are the first LysR-type regulators to be structurally characterized while bound with physiologically relevant exogenous inducers. The effector complexes were obtained by soaking crystals with stabilizing solutions containing high effector concentrations and minimal amounts of competing ions. This strategy, including data collection with fragments of fractured crystals, may be generally applicable to related proteins. In BenM and CatM, the binding of muconate to an interdomain pocket was facilitated by helix dipoles that provide charge stabilization. In BenM, benzoate also bound in an adjacent hydrophobic region where it alters the effect of muconate bound in the primary site. A charge relay system within the BenM protein appears to underlie synergistic transcriptional activation. According to this model, Glu162 is a pivotal residue that forms salt-bridges with different arginine residues depending on the occupancy of the secondary effector-binding site. Glu162 interacts with Arg160 in the absence of benzoate and with Arg146 when benzoate is bound. This latter interaction enhances the negative charge of muconate bound to the adjacent primary effector-binding site. The redistribution of the electrostatic potential draws two domains of the protein more closely towards muconate, with the movement mediated by the dipole moments of four alpha helices. Therefore, with both effectors, BenM achieves a unique conformation capable of high level transcriptional activation.
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'''CatM effector binding domain with its effector cis,cis-muconate'''
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Distinct effector-binding sites enable synergistic transcriptional activation by BenM, a LysR-type regulator.,Ezezika OC, Haddad S, Clark TJ, Neidle EL, Momany C J Mol Biol. 2007 Mar 30;367(3):616-29. Epub 2006 Oct 4. PMID:17291527<ref>PMID:17291527</ref>
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==Overview==
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BenM, a bacterial transcriptional regulator, responds synergistically to two effectors, benzoate and cis,cis-muconate. CatM, a paralog with overlapping function, responds only to muconate. Structures of their effector-binding domains revealed two effector-binding sites in BenM. BenM and CatM are the first LysR-type regulators to be structurally characterized while bound with physiologically relevant exogenous inducers. The effector complexes were obtained by soaking crystals with stabilizing solutions containing high effector concentrations and minimal amounts of competing ions. This strategy, including data collection with fragments of fractured crystals, may be generally applicable to related proteins. In BenM and CatM, the binding of muconate to an interdomain pocket was facilitated by helix dipoles that provide charge stabilization. In BenM, benzoate also bound in an adjacent hydrophobic region where it alters the effect of muconate bound in the primary site. A charge relay system within the BenM protein appears to underlie synergistic transcriptional activation. According to this model, Glu162 is a pivotal residue that forms salt-bridges with different arginine residues depending on the occupancy of the secondary effector-binding site. Glu162 interacts with Arg160 in the absence of benzoate and with Arg146 when benzoate is bound. This latter interaction enhances the negative charge of muconate bound to the adjacent primary effector-binding site. The redistribution of the electrostatic potential draws two domains of the protein more closely towards muconate, with the movement mediated by the dipole moments of four alpha helices. Therefore, with both effectors, BenM achieves a unique conformation capable of high level transcriptional activation.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2F7C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baylyi Acinetobacter baylyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F7C OCA].
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</div>
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<div class="pdbe-citations 2f7c" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Distinct effector-binding sites enable synergistic transcriptional activation by BenM, a LysR-type regulator., Ezezika OC, Haddad S, Clark TJ, Neidle EL, Momany C, J Mol Biol. 2007 Mar 30;367(3):616-29. Epub 2006 Oct 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17291527 17291527]
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Acinetobacter baylyi]]
[[Category: Acinetobacter baylyi]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Clark, T.]]
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[[Category: Clark T]]
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[[Category: Ezezika, O.]]
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[[Category: Ezezika O]]
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[[Category: Haddad, S.]]
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[[Category: Haddad S]]
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[[Category: Momany, C.]]
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[[Category: Momany C]]
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[[Category: Neidle, E.]]
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[[Category: Neidle E]]
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[[Category: Effector binding domain]]
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[[Category: Inducer binding domain]]
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[[Category: Lttr]]
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[[Category: Lysr-type transcriptional regulator]]
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[[Category: Muconate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:33:08 2008''
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Current revision

CatM effector binding domain with its effector cis,cis-muconate

PDB ID 2f7c

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