1pm4

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(New page: 200px<br /><applet load="1pm4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pm4, resolution 1.755&Aring;" /> '''Crystal structure o...)
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[[Image:1pm4.gif|left|200px]]<br /><applet load="1pm4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pm4, resolution 1.755&Aring;" />
caption="1pm4, resolution 1.755&Aring;" />
'''Crystal structure of Yersinia pseudotuberculosis-derived mitogen (YPM)'''<br />
'''Crystal structure of Yersinia pseudotuberculosis-derived mitogen (YPM)'''<br />
==Overview==
==Overview==
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Superantigens are a class of microbial proteins with the ability to, excessively activate T cells by binding to the T cell receptor. The, staphylococcal and streptococcal superantigens are closely related in, structure and possess an N-terminal domain that resembles an OB fold and a, C-terminal domain similar to a beta-grasp fold. Yersinia, pseudotuberculosis produces superantigens, YPMa, YPMb, and YPMc, which, have no significant amino acid similarity to other proteins. We have, determined the crystal and solution structures of YPMa, which show that, the protein has a jelly-roll fold. The closest structural neighbors to, YPMa are viral capsid proteins and members of the tumor necrosis factor, superfamily. In the crystal structure, YPMa packs as a trimer, another, feature shared with viral capsid proteins and TNF superfamily proteins., However, in solution YPMa behaves as a monomer, and any functional, relevance of the trimer observed in the crystals is yet to be established.
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Superantigens are a class of microbial proteins with the ability to excessively activate T cells by binding to the T cell receptor. The staphylococcal and streptococcal superantigens are closely related in structure and possess an N-terminal domain that resembles an OB fold and a C-terminal domain similar to a beta-grasp fold. Yersinia pseudotuberculosis produces superantigens, YPMa, YPMb, and YPMc, which have no significant amino acid similarity to other proteins. We have determined the crystal and solution structures of YPMa, which show that the protein has a jelly-roll fold. The closest structural neighbors to YPMa are viral capsid proteins and members of the tumor necrosis factor superfamily. In the crystal structure, YPMa packs as a trimer, another feature shared with viral capsid proteins and TNF superfamily proteins. However, in solution YPMa behaves as a monomer, and any functional relevance of the trimer observed in the crystals is yet to be established.
==About this Structure==
==About this Structure==
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1PM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PM4 OCA].
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1PM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PM4 OCA].
==Reference==
==Reference==
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[[Category: Yersinia pseudotuberculosis]]
[[Category: Yersinia pseudotuberculosis]]
[[Category: Donadini, R.]]
[[Category: Donadini, R.]]
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[[Category: Fields, B.A.]]
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[[Category: Fields, B A.]]
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[[Category: Kwan, A.H.]]
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[[Category: Kwan, A H.]]
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[[Category: Liew, C.W.]]
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[[Category: Liew, C W.]]
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[[Category: Mackay, J.P.]]
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[[Category: Mackay, J P.]]
[[Category: jelly roll fold]]
[[Category: jelly roll fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:41:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:12 2008''

Revision as of 12:30, 21 February 2008


1pm4, resolution 1.755Å

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Crystal structure of Yersinia pseudotuberculosis-derived mitogen (YPM)

Overview

Superantigens are a class of microbial proteins with the ability to excessively activate T cells by binding to the T cell receptor. The staphylococcal and streptococcal superantigens are closely related in structure and possess an N-terminal domain that resembles an OB fold and a C-terminal domain similar to a beta-grasp fold. Yersinia pseudotuberculosis produces superantigens, YPMa, YPMb, and YPMc, which have no significant amino acid similarity to other proteins. We have determined the crystal and solution structures of YPMa, which show that the protein has a jelly-roll fold. The closest structural neighbors to YPMa are viral capsid proteins and members of the tumor necrosis factor superfamily. In the crystal structure, YPMa packs as a trimer, another feature shared with viral capsid proteins and TNF superfamily proteins. However, in solution YPMa behaves as a monomer, and any functional relevance of the trimer observed in the crystals is yet to be established.

About this Structure

1PM4 is a Single protein structure of sequence from Yersinia pseudotuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal and solution structures of a superantigen from Yersinia pseudotuberculosis reveal a jelly-roll fold., Donadini R, Liew CW, Kwan AH, Mackay JP, Fields BA, Structure. 2004 Jan;12(1):145-56. PMID:14725774

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