2axc: Difference between revisions

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New page: left|200px<br /><applet load="2axc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2axc, resolution 1.70Å" /> '''Crystal structure of...
 
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[[Image:2axc.gif|left|200px]]<br /><applet load="2axc" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2axc.gif|left|200px]]<br /><applet load="2axc" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2axc, resolution 1.70&Aring;" />
caption="2axc, resolution 1.70&Aring;" />
'''Crystal structure of ColE7 translocation domain'''<br />
'''Crystal structure of ColE7 translocation domain'''<br />


==Overview==
==Overview==
ColE7 is a nuclease-type colicin released from Escherichia coli to kill, sensitive bacterial cells by degrading the nucleic acid molecules in their, cytoplasm. ColE7 is classified as one of the group A colicins, since the, N-terminal translocation domain (T-domain) of the nuclease-type colicins, interact with specific membrane-bound or periplasmic Tol proteins during, protein import. Here, we show that if the N-terminal tail of ColE7 is, deleted, ColE7 (residues 63-576) loses its bactericidal activity against, E.coli. Moreover, TolB protein interacts directly with the T-domain of, ColE7 (residues 1-316), but not with the N-terminal deleted T-domain, (residues 60-316), as detected by co-immunoprecipitation experiments, confirming that the N-terminal tail is required for ColE7 interactions, with TolB. The crystal structure of the N-terminal tail deleted ColE7, T-domain was determined by the multi-wavelength anomalous dispersion, method at a resolution of 1.7 angstroms. The structure of the ColE7, T-domain superimposes well with the T-domain of ColE3 and TR-domain of, ColB, a group A Tol-dependent colicin and a group B TonB-dependent, colicin, respectively. The structural resemblance of group A and B, colicins implies that the two groups of colicins may share a mechanistic, connection during cellular import.
ColE7 is a nuclease-type colicin released from Escherichia coli to kill sensitive bacterial cells by degrading the nucleic acid molecules in their cytoplasm. ColE7 is classified as one of the group A colicins, since the N-terminal translocation domain (T-domain) of the nuclease-type colicins interact with specific membrane-bound or periplasmic Tol proteins during protein import. Here, we show that if the N-terminal tail of ColE7 is deleted, ColE7 (residues 63-576) loses its bactericidal activity against E.coli. Moreover, TolB protein interacts directly with the T-domain of ColE7 (residues 1-316), but not with the N-terminal deleted T-domain (residues 60-316), as detected by co-immunoprecipitation experiments, confirming that the N-terminal tail is required for ColE7 interactions with TolB. The crystal structure of the N-terminal tail deleted ColE7 T-domain was determined by the multi-wavelength anomalous dispersion method at a resolution of 1.7 angstroms. The structure of the ColE7 T-domain superimposes well with the T-domain of ColE3 and TR-domain of ColB, a group A Tol-dependent colicin and a group B TonB-dependent colicin, respectively. The structural resemblance of group A and B colicins implies that the two groups of colicins may share a mechanistic connection during cellular import.


==About this Structure==
==About this Structure==
2AXC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AXC OCA].  
2AXC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXC OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chak, K.F.]]
[[Category: Chak, K F.]]
[[Category: Cheng, Y.S.]]
[[Category: Cheng, Y S.]]
[[Category: Doudeva, L.G.]]
[[Category: Doudeva, L G.]]
[[Category: Shi, Z.]]
[[Category: Shi, Z.]]
[[Category: Yang, W.Z.]]
[[Category: Yang, W Z.]]
[[Category: Yuan, H.S.]]
[[Category: Yuan, H S.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: translocation domain]]
[[Category: translocation domain]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:25:57 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:59 2008''

Revision as of 17:31, 21 February 2008

File:2axc.gif


2axc, resolution 1.70Å

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Crystal structure of ColE7 translocation domain

OverviewOverview

ColE7 is a nuclease-type colicin released from Escherichia coli to kill sensitive bacterial cells by degrading the nucleic acid molecules in their cytoplasm. ColE7 is classified as one of the group A colicins, since the N-terminal translocation domain (T-domain) of the nuclease-type colicins interact with specific membrane-bound or periplasmic Tol proteins during protein import. Here, we show that if the N-terminal tail of ColE7 is deleted, ColE7 (residues 63-576) loses its bactericidal activity against E.coli. Moreover, TolB protein interacts directly with the T-domain of ColE7 (residues 1-316), but not with the N-terminal deleted T-domain (residues 60-316), as detected by co-immunoprecipitation experiments, confirming that the N-terminal tail is required for ColE7 interactions with TolB. The crystal structure of the N-terminal tail deleted ColE7 T-domain was determined by the multi-wavelength anomalous dispersion method at a resolution of 1.7 angstroms. The structure of the ColE7 T-domain superimposes well with the T-domain of ColE3 and TR-domain of ColB, a group A Tol-dependent colicin and a group B TonB-dependent colicin, respectively. The structural resemblance of group A and B colicins implies that the two groups of colicins may share a mechanistic connection during cellular import.

About this StructureAbout this Structure

2AXC is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

High-resolution crystal structure of a truncated ColE7 translocation domain: implications for colicin transport across membranes., Cheng YS, Shi Z, Doudeva LG, Yang WZ, Chak KF, Yuan HS, J Mol Biol. 2006 Feb 10;356(1):22-31. Epub 2005 Dec 5. PMID:16360169

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