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New page: left|200px<br /><applet load="1jbg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jbg, resolution 2.75Å" /> '''Crystal Structure of...
 
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[[Image:1jbg.jpg|left|200px]]<br /><applet load="1jbg" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of MtaN, the Bacillus subtilis Multidrug Transporter Activator, N-terminus'''<br />


==Overview==
==Crystal Structure of MtaN, the Bacillus subtilis Multidrug Transporter Activator, N-terminus==
MtaN (Multidrug Transporter Activation, N terminus) is a constitutive, transcriptionally active 109-residue truncation mutant, which contains, only the N-terminal DNA-binding and dimerization domains of MerR family, member Mta. The 2.75 A resolution crystal structure of apo-MtaN reveals a, winged helix-turn-helix protein with a protruding 8-turn helix (alpha5), that is involved in dimerization by the formation of an antiparallel, coiled-coil. The hydrophobic core and helices alpha1 through alpha4 are, structurally homologous to MerR family member BmrR bound to DNA, whereas, one wing (Wing 1) is shifted. Differences between the orientation of, alpha5 with respect to the core and the revolution of the antiparallel, coiled-coil lead to significantly altered conformations of MtaN and BmrR, dimers. These shifts result in a conformation of MtaN that appears to be, incompatible with the transcription activation mechanism of BmrR and, suggest that additional DNA-induced structural changes are necessary.
<StructureSection load='1jbg' size='340' side='right'caption='[[1jbg]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1jbg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JBG FirstGlance]. <br>
1JBG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JBG OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#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=1jbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jbg OCA], [https://pdbe.org/1jbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jbg RCSB], [https://www.ebi.ac.uk/pdbsum/1jbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jbg ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structure of MtaN, a global multidrug transporter gene activator., Godsey MH, Baranova NN, Neyfakh AA, Brennan RG, J Biol Chem. 2001 Dec 14;276(50):47178-84. Epub 2001 Oct 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11581256 11581256]
== Function ==
[https://www.uniprot.org/uniprot/MTA_BACSU MTA_BACSU] Global transcriptional regulator that activates transcription of bmr and blt by binding directly to their promoter. Stimulates also the expression of the mta gene itself, ydfK and ymfE.<ref>PMID:10200972</ref> <ref>PMID:18502870</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/1jbg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1jbg ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brennan, R.G.]]
[[Category: Brennan RG]]
[[Category: Godsey, M.H.]]
[[Category: Godsey MH]]
[[Category: Neyfakh, A.A.]]
[[Category: Neyfakh AA]]
[[Category: antiparallel coiled-coil]]
[[Category: winged helix-turn-helix]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:24:44 2007''

Latest revision as of 10:38, 7 February 2024

Crystal Structure of MtaN, the Bacillus subtilis Multidrug Transporter Activator, N-terminusCrystal Structure of MtaN, the Bacillus subtilis Multidrug Transporter Activator, N-terminus

Structural highlights

1jbg is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.75Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MTA_BACSU Global transcriptional regulator that activates transcription of bmr and blt by binding directly to their promoter. Stimulates also the expression of the mta gene itself, ydfK and ymfE.[1] [2]

Evolutionary Conservation

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

References

  1. ↑ Baranova NN, Danchin A, Neyfakh AA. Mta, a global MerR-type regulator of the Bacillus subtilis multidrug-efflux transporters. Mol Microbiol. 1999 Mar;31(5):1549-59. PMID:10200972
  2. ↑ Miethke M, Schmidt S, Marahiel MA. The major facilitator superfamily-type transporter YmfE and the multidrug-efflux activator Mta mediate bacillibactin secretion in Bacillus subtilis. J Bacteriol. 2008 Aug;190(15):5143-52. Epub 2008 May 23. PMID:18502870 doi:http://dx.doi.org/JB.00464-08

1jbg, resolution 2.75Å

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