1z0r

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(New page: 200px<br /><applet load="1z0r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z0r" /> '''Solution Structure of the N-terminal DNA Rec...)
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'''Solution Structure of the N-terminal DNA Recognition Domain of the Bacillus subtilis Transcription-State Regulator AbrB'''<br />
'''Solution Structure of the N-terminal DNA Recognition Domain of the Bacillus subtilis Transcription-State Regulator AbrB'''<br />
==Overview==
==Overview==
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New relationships found in the process of updating the structural, classification of proteins (SCOP) database resulted in the revision of the, structure of the N-terminal, DNA-binding domain of the transition state, regulator AbrB. The dimeric AbrB domain shares a common fold with the, addiction antidote MazE and the subunit of uncharacterized protein MraZ, implicated in cell division and cell envelope formation. It has a, detectable sequence similarity to both MazE and MraZ thus providing an, evolutionary link between the two proteins. The putative DNA-binding site, of AbrB is found on the same face as the DNA-binding site of MazE and, appears similar, both in structure and sequence, to the exposed conserved, region of MraZ. This strongly suggests that MraZ also binds DNA and allows, for a consensus model of DNA recognition by the members of this novel, protein superfamily.
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New relationships found in the process of updating the structural classification of proteins (SCOP) database resulted in the revision of the structure of the N-terminal, DNA-binding domain of the transition state regulator AbrB. The dimeric AbrB domain shares a common fold with the addiction antidote MazE and the subunit of uncharacterized protein MraZ implicated in cell division and cell envelope formation. It has a detectable sequence similarity to both MazE and MraZ thus providing an evolutionary link between the two proteins. The putative DNA-binding site of AbrB is found on the same face as the DNA-binding site of MazE and appears similar, both in structure and sequence, to the exposed conserved region of MraZ. This strongly suggests that MraZ also binds DNA and allows for a consensus model of DNA recognition by the members of this novel protein superfamily.
==About this Structure==
==About this Structure==
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1Z0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. This structure superseeds the now removed PDB entry 1EKT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z0R OCA].
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1Z0R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. This structure supersedes the now removed PDB entry 1EKT. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0R OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Andreeva, A.]]
[[Category: Andreeva, A.]]
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[[Category: Bobay, B.G.]]
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[[Category: Bobay, B G.]]
[[Category: Cavanagh, J.]]
[[Category: Cavanagh, J.]]
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[[Category: Mueller, G.A.]]
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[[Category: Mueller, G A.]]
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[[Category: Murzin, A.G.]]
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[[Category: Murzin, A G.]]
[[Category: n-terminal dna-binding domain]]
[[Category: n-terminal dna-binding domain]]
[[Category: scop database]]
[[Category: scop database]]
[[Category: transition state regulator]]
[[Category: transition state regulator]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:10:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:01 2008''

Revision as of 14:11, 21 February 2008


1z0r

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Solution Structure of the N-terminal DNA Recognition Domain of the Bacillus subtilis Transcription-State Regulator AbrB

Overview

New relationships found in the process of updating the structural classification of proteins (SCOP) database resulted in the revision of the structure of the N-terminal, DNA-binding domain of the transition state regulator AbrB. The dimeric AbrB domain shares a common fold with the addiction antidote MazE and the subunit of uncharacterized protein MraZ implicated in cell division and cell envelope formation. It has a detectable sequence similarity to both MazE and MraZ thus providing an evolutionary link between the two proteins. The putative DNA-binding site of AbrB is found on the same face as the DNA-binding site of MazE and appears similar, both in structure and sequence, to the exposed conserved region of MraZ. This strongly suggests that MraZ also binds DNA and allows for a consensus model of DNA recognition by the members of this novel protein superfamily.

About this Structure

1Z0R is a Single protein structure of sequence from Bacillus subtilis. This structure supersedes the now removed PDB entry 1EKT. Full crystallographic information is available from OCA.

Reference

Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins., Bobay BG, Andreeva A, Mueller GA, Cavanagh J, Murzin AG, FEBS Lett. 2005 Oct 24;579(25):5669-74. Epub 2005 Oct 4. PMID:16223496

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