1t5e

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(New page: 200px<br /><applet load="1t5e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t5e, resolution 3.&Aring;" /> '''The structure of MexA'...)
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[[Image:1t5e.gif|left|200px]]<br /><applet load="1t5e" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t5e, resolution 3.&Aring;" />
caption="1t5e, resolution 3.&Aring;" />
'''The structure of MexA'''<br />
'''The structure of MexA'''<br />
==Overview==
==Overview==
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Multidrug resistance among Gram-negative bacteria is conferred by, three-component membrane pumps that expel diverse antibiotics from the, cell. These efflux pumps consist of an inner membrane transporter such as, the AcrB proton antiporter, an outer membrane exit duct of the TolC, family, and a periplasmic protein known as the adaptor. We present the, x-ray structure of the MexA adaptor from the human pathogen Pseudomonas, aeruginosa. The elongated molecule contains three linearly arranged, subdomains; a 47-A-long alpha-helical hairpin, a lipoyl domain, and a, six-stranded beta-barrel. In the crystal, hairpins of neighboring MexA, monomers pack side-by-side to form twisted arcs. We discuss the, implications of the packing of molecules within the crystal. On the basis, of the structure and packing, we suggest a model for the key periplasmic, interaction between the outer membrane channel and the adaptor protein in, the assembled drug efflux pump.
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Multidrug resistance among Gram-negative bacteria is conferred by three-component membrane pumps that expel diverse antibiotics from the cell. These efflux pumps consist of an inner membrane transporter such as the AcrB proton antiporter, an outer membrane exit duct of the TolC family, and a periplasmic protein known as the adaptor. We present the x-ray structure of the MexA adaptor from the human pathogen Pseudomonas aeruginosa. The elongated molecule contains three linearly arranged subdomains; a 47-A-long alpha-helical hairpin, a lipoyl domain, and a six-stranded beta-barrel. In the crystal, hairpins of neighboring MexA monomers pack side-by-side to form twisted arcs. We discuss the implications of the packing of molecules within the crystal. On the basis of the structure and packing, we suggest a model for the key periplasmic interaction between the outer membrane channel and the adaptor protein in the assembled drug efflux pump.
==About this Structure==
==About this Structure==
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1T5E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with 3GR 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=1T5E OCA].
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1T5E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=3GR:'>3GR</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=1T5E OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bokma, E.]]
[[Category: Bokma, E.]]
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[[Category: Higgins, M.K.]]
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[[Category: Higgins, M K.]]
[[Category: Hughes, C.]]
[[Category: Hughes, C.]]
[[Category: Koronakis, E.]]
[[Category: Koronakis, E.]]
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[[Category: periplasmic adaptor protein]]
[[Category: periplasmic adaptor protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:00:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:03 2008''

Revision as of 13:10, 21 February 2008


1t5e, resolution 3.Å

Drag the structure with the mouse to rotate

The structure of MexA

Overview

Multidrug resistance among Gram-negative bacteria is conferred by three-component membrane pumps that expel diverse antibiotics from the cell. These efflux pumps consist of an inner membrane transporter such as the AcrB proton antiporter, an outer membrane exit duct of the TolC family, and a periplasmic protein known as the adaptor. We present the x-ray structure of the MexA adaptor from the human pathogen Pseudomonas aeruginosa. The elongated molecule contains three linearly arranged subdomains; a 47-A-long alpha-helical hairpin, a lipoyl domain, and a six-stranded beta-barrel. In the crystal, hairpins of neighboring MexA monomers pack side-by-side to form twisted arcs. We discuss the implications of the packing of molecules within the crystal. On the basis of the structure and packing, we suggest a model for the key periplasmic interaction between the outer membrane channel and the adaptor protein in the assembled drug efflux pump.

About this Structure

1T5E is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the periplasmic component of a bacterial drug efflux pump., Higgins MK, Bokma E, Koronakis E, Hughes C, Koronakis V, Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):9994-9. Epub 2004 Jun 28. PMID:15226509

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