1k6z

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(New page: 200px<br /><applet load="1k6z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k6z, resolution 2.0&Aring;" /> '''Crystal Structure of ...)
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[[Image:1k6z.jpg|left|200px]]<br /><applet load="1k6z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1k6z, resolution 2.0&Aring;" />
caption="1k6z, resolution 2.0&Aring;" />
'''Crystal Structure of the Yersinia Secretion Chaperone SycE'''<br />
'''Crystal Structure of the Yersinia Secretion Chaperone SycE'''<br />
==Overview==
==Overview==
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Many bacterial pathogens utilize a type III (contact-dependent) secretion, system to inject cytotoxic effector proteins directly into host cells., This ingenious mechanism, designed for both bacterial offense and defense, has been studied most extensively in Yersinia spp. To be exported, efficiently, at least three of the effectors (YopE, YopH and YopT) and, several other proteins that transit the type III secretion pathway in, Yersinia (YopN, YopD and YopB) must first form transient complexes with, cognate-specific Yop chaperone (Syc) proteins. The cytotoxic effector, YopE, a selective activator of mammalian Rho-family GTPases, associates, with SycE. Here, the structure of Y. pestis SycE at 1.95A resolution is, reported. SycE possesses a novel fold with an unusual dimerization motif, and an intriguing basic cavity located on the dyad axis of the dimer that, may participate in its interaction with YopE.
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Many bacterial pathogens utilize a type III (contact-dependent) secretion system to inject cytotoxic effector proteins directly into host cells. This ingenious mechanism, designed for both bacterial offense and defense, has been studied most extensively in Yersinia spp. To be exported efficiently, at least three of the effectors (YopE, YopH and YopT) and several other proteins that transit the type III secretion pathway in Yersinia (YopN, YopD and YopB) must first form transient complexes with cognate-specific Yop chaperone (Syc) proteins. The cytotoxic effector YopE, a selective activator of mammalian Rho-family GTPases, associates with SycE. Here, the structure of Y. pestis SycE at 1.95A resolution is reported. SycE possesses a novel fold with an unusual dimerization motif and an intriguing basic cavity located on the dyad axis of the dimer that may participate in its interaction with YopE.
==About this Structure==
==About this Structure==
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1K6Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis] with IMD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K6Z OCA].
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1K6Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis] with <scene name='pdbligand=IMD:'>IMD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6Z OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Yersinia pestis]]
[[Category: Yersinia pestis]]
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[[Category: Evdokimov, A.G.]]
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[[Category: Evdokimov, A G.]]
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[[Category: Routzahn, K.M.]]
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[[Category: Routzahn, K M.]]
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[[Category: Tropea, J.E.]]
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[[Category: Tropea, J E.]]
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[[Category: Waugh, D.S.]]
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[[Category: Waugh, D S.]]
[[Category: IMD]]
[[Category: IMD]]
[[Category: chaperone]]
[[Category: chaperone]]
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[[Category: yersinia pestis]]
[[Category: yersinia pestis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:53:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:48 2008''

Revision as of 11:30, 21 February 2008


1k6z, resolution 2.0Å

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Crystal Structure of the Yersinia Secretion Chaperone SycE

Overview

Many bacterial pathogens utilize a type III (contact-dependent) secretion system to inject cytotoxic effector proteins directly into host cells. This ingenious mechanism, designed for both bacterial offense and defense, has been studied most extensively in Yersinia spp. To be exported efficiently, at least three of the effectors (YopE, YopH and YopT) and several other proteins that transit the type III secretion pathway in Yersinia (YopN, YopD and YopB) must first form transient complexes with cognate-specific Yop chaperone (Syc) proteins. The cytotoxic effector YopE, a selective activator of mammalian Rho-family GTPases, associates with SycE. Here, the structure of Y. pestis SycE at 1.95A resolution is reported. SycE possesses a novel fold with an unusual dimerization motif and an intriguing basic cavity located on the dyad axis of the dimer that may participate in its interaction with YopE.

About this Structure

1K6Z is a Single protein structure of sequence from Yersinia pestis with as ligand. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of the type III secretion chaperone SycE from Yersinia pestis., Evdokimov AG, Tropea JE, Routzahn KM, Waugh DS, Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):398-406. Epub 2002, Feb 21. PMID:11856824

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