2amj: Difference between revisions

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==Crystal Structure of Modulator of Drug Activity B from Escherichia coli O157:H7==
==Crystal Structure of Modulator of Drug Activity B from Escherichia coli O157:H7==
<StructureSection load='2amj' size='340' side='right' caption='[[2amj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2amj' size='340' side='right'caption='[[2amj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2amj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AMJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AMJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2amj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AMJ FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b3d|2b3d]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b3d|2b3d]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mdaB, mda66 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mdaB, mda66 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=2amj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2amj OCA], [http://pdbe.org/2amj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2amj RCSB], [http://www.ebi.ac.uk/pdbsum/2amj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2amj ProSAT], [http://www.topsan.org/Proteins/BSGI/2amj TOPSAN]</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=2amj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2amj OCA], [https://pdbe.org/2amj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2amj RCSB], [https://www.ebi.ac.uk/pdbsum/2amj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2amj ProSAT], [https://www.topsan.org/Proteins/BSGI/2amj TOPSAN]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/am/2amj_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/am/2amj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 33: Line 33:
</StructureSection>
</StructureSection>
[[Category: Eco57]]
[[Category: Eco57]]
[[Category: Large Structures]]
[[Category: Adams, M A]]
[[Category: Adams, M A]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

Revision as of 11:33, 27 January 2021

Crystal Structure of Modulator of Drug Activity B from Escherichia coli O157:H7Crystal Structure of Modulator of Drug Activity B from Escherichia coli O157:H7

Structural highlights

2amj is a 4 chain structure with sequence from Eco57. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:mdaB, mda66 (ECO57)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Evolutionary Conservation

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

Publication Abstract from PubMed

Modulator of drug activity B (MdaB) is a putative member of the DT-diaphorase family of NAD(P)H:oxidoreductases that afford cellular protection against quinonoid compounds. While there have been extensive investigations of mammalian homologues, putative prokaryotic members of this enzyme family have received little attention. The three-dimensional crystal structure of apo-MdaB reported herein exhibits significant structural similarity to a number of flavoproteins, including the mammalian DT-diaphorases. We have shown by mass spectrometry that the endogenously associated cofactor is flavin adenine dinucleotide and we present here the structure of MdaB in complex with this compound. Growth of Escherichia coli carrying null mutations in the genes encoding MdaB or quinol monooxygenase, the gene for which shares the mdaB promoter, were not affected by the presence of menadione. However, over-expression of recombinant quinol monooxygenase conferred a state of resistance against both tetracycline and adriamycin. This work suggests that the redox cycle formed by these proteins protects E. coli from the toxic effects of polyketide compounds rather than the oxidative stress of menadione alone.

Modulator of drug activity B from Escherichia coli: crystal structure of a prokaryotic homologue of DT-diaphorase.,Adams MA, Jia Z J Mol Biol. 2006 Jun 2;359(2):455-65. Epub 2006 Apr 7. PMID:16630630[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Adams MA, Jia Z. Modulator of drug activity B from Escherichia coli: crystal structure of a prokaryotic homologue of DT-diaphorase. J Mol Biol. 2006 Jun 2;359(2):455-65. Epub 2006 Apr 7. PMID:16630630 doi:10.1016/j.jmb.2006.03.053

2amj, resolution 1.80Å

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