1bl0: Difference between revisions

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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 ==
<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 [https://proteopedia.org/fgij/fg.htm?mol=1BL0 FirstGlance]. <br>
<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>
</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=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>
</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>
<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 ==
[[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.  
[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>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bl0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Davies, S]]
[[Category: Davies S]]
[[Category: Martin, J L]]
[[Category: Martin JL]]
[[Category: Rhee, R G]]
[[Category: Rhee RG]]
[[Category: Rosner, D R]]
[[Category: Rosner DR]]
[[Category: A bipartite helix-turn-helix protein]]
[[Category: Transcription-dna complex]]
[[Category: Transcriptional activator]]

Latest revision as of 09:37, 7 February 2024

MULTIPLE ANTIBIOTIC RESISTANCE PROTEIN (MARA)/DNA COMPLEXMULTIPLE ANTIBIOTIC RESISTANCE PROTEIN (MARA)/DNA COMPLEX

Structural highlights

1bl0 is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1bl0, resolution 2.30Å

Drag the structure with the mouse to rotate

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OCA
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