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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"  
[[Image:1jbg.jpg|left|200px]]<br /><applet load="1jbg" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jbg, resolution 2.75&Aring;" />
caption="1jbg, resolution 2.75&Aring;" />
'''Crystal Structure of MtaN, the Bacillus subtilis Multidrug Transporter Activator, N-terminus'''<br />
'''Crystal Structure of MtaN, the Bacillus subtilis Multidrug Transporter Activator, N-terminus'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
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].  
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://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBG OCA].  


==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brennan, R.G.]]
[[Category: Brennan, R G.]]
[[Category: Godsey, M.H.]]
[[Category: Godsey, M H.]]
[[Category: Neyfakh, A.A.]]
[[Category: Neyfakh, A A.]]
[[Category: antiparallel coiled-coil]]
[[Category: antiparallel coiled-coil]]
[[Category: winged helix-turn-helix]]
[[Category: winged helix-turn-helix]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:24:44 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:44 2008''