1bl0

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<StructureSection load='1bl0' size='340' side='right'caption='[[1bl0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1bl0' size='340' side='right'caption='[[1bl0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1bl0]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BL0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1bl0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BL0 FirstGlance]. <br>
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</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=1bl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bl0 OCA], [http://pdbe.org/1bl0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bl0 RCSB], [http://www.ebi.ac.uk/pdbsum/1bl0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bl0 ProSAT]</span></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]] 2.3&#8491;</td></tr>
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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=1bl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bl0 OCA], [https://pdbe.org/1bl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bl0 RCSB], [https://www.ebi.ac.uk/pdbsum/1bl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bl0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MARA_ECOLI MARA_ECOLI]] May be a transcriptional activator of genes involved in the multiple antibiotic resistance (Mar) phenotype. It can also activate genes such as sodA, zwf and micF.
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[https://www.uniprot.org/uniprot/MARA_ECOLI MARA_ECOLI] May be a transcriptional activator of genes involved in the multiple antibiotic resistance (Mar) phenotype. It can also activate genes such as sodA, zwf and micF.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1bl0 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=1bl0 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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A crystal structure for a member of the AraC prokaryotic transcriptional activator family, MarA, in complex with its cognate DNA-binding site is described. MarA consists of two similar subdomains, each containing a helix-turn-helix DNA-binding motif. The two recognition helices of the motifs are inserted into adjacent major groove segments on the same face of the DNA but are separated by only 27 A thereby bending the DNA by approximately 35 degrees. Extensive interactions between the recognition helices and the DNA major groove provide the sequence specificity.
 
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A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator.,Rhee S, Martin RG, Rosner JL, Davies DR Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10413-8. PMID:9724717<ref>PMID:9724717</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 1bl0" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Davies, S]]
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[[Category: Davies S]]
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[[Category: Martin, J L]]
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[[Category: Martin JL]]
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[[Category: Rhee, R G]]
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[[Category: Rhee RG]]
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[[Category: Rosner, D R]]
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[[Category: Rosner DR]]
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[[Category: A bipartite helix-turn-helix protein]]
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[[Category: Transcription-dna complex]]
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[[Category: Transcriptional activator]]
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Current revision

MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN (MARA)/DNA COMPLEX

PDB ID 1bl0

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