2d27

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(New page: 200px<br /><applet load="2d27" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d27, resolution 2.210&Aring;" /> '''Structure of the N-...)
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caption="2d27, resolution 2.210&Aring;" />
caption="2d27, resolution 2.210&Aring;" />
'''Structure of the N-terminal domain of XpsE (crystal form I4122)'''<br />
'''Structure of the N-terminal domain of XpsE (crystal form I4122)'''<br />
==Overview==
==Overview==
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Secretion of fully folded extracellular proteins across the outer membrane, of Gram-negative bacteria is mainly assisted by the ATP-dependent type II, secretion system (T2SS). Depending on species, 12-15 proteins are usually, required for the function of T2SS by forming a trans-envelope multiprotein, secretion complex. Here we report crystal structures of an essential, component of the Xanthomonas campestris T2SS, the 21-kDa N-terminal domain, of cytosolic secretion ATPase XpsE (XpsEN), in two conformational states., By mediating interaction between XpsE and the cytoplasmic membrane protein, XpsL, XpsEN anchors XpsE to the membrane-associated secretion complex to, allow the coupling between ATP utilization and exoprotein secretion. The, structure of XpsEN observed in crystal form P4(3)2(1)2 is composed of a, 90-residue alpha/beta sandwich core domain capped by a 62-residue, N-terminal helical region. The core domain exhibits structural similarity, with the NifU-like domain, suggesting that XpsE(N) may be involved in the, regulation of XpsE ATPase activity. Surprisingly, although a similar core, domain structure was observed in crystal form I4(1)22, the N-terminal 36, residues of the helical region undergo a large structural rearrangement., Deletion analysis indicates that these residues are required for, exoprotein secretion by mediating the XpsE/XpsL interaction. Site-directed, mutagenesis study further suggests the more compact conformation observed, in the P4(3)2(1)2 crystal likely represents the XpsL binding-competent, state. Based on these findings, we speculate that XpsE might function in, T2SS by cycling between two conformational states. As a closely related, protein to XpsE, secretion ATPase PilB may function similarly in the type, IV pilus assembly.
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Secretion of fully folded extracellular proteins across the outer membrane of Gram-negative bacteria is mainly assisted by the ATP-dependent type II secretion system (T2SS). Depending on species, 12-15 proteins are usually required for the function of T2SS by forming a trans-envelope multiprotein secretion complex. Here we report crystal structures of an essential component of the Xanthomonas campestris T2SS, the 21-kDa N-terminal domain of cytosolic secretion ATPase XpsE (XpsEN), in two conformational states. By mediating interaction between XpsE and the cytoplasmic membrane protein XpsL, XpsEN anchors XpsE to the membrane-associated secretion complex to allow the coupling between ATP utilization and exoprotein secretion. The structure of XpsEN observed in crystal form P4(3)2(1)2 is composed of a 90-residue alpha/beta sandwich core domain capped by a 62-residue N-terminal helical region. The core domain exhibits structural similarity with the NifU-like domain, suggesting that XpsE(N) may be involved in the regulation of XpsE ATPase activity. Surprisingly, although a similar core domain structure was observed in crystal form I4(1)22, the N-terminal 36 residues of the helical region undergo a large structural rearrangement. Deletion analysis indicates that these residues are required for exoprotein secretion by mediating the XpsE/XpsL interaction. Site-directed mutagenesis study further suggests the more compact conformation observed in the P4(3)2(1)2 crystal likely represents the XpsL binding-competent state. Based on these findings, we speculate that XpsE might function in T2SS by cycling between two conformational states. As a closely related protein to XpsE, secretion ATPase PilB may function similarly in the type IV pilus assembly.
==About this Structure==
==About this Structure==
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2D27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D27 OCA].
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2D27 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D27 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Xanthomonas campestris]]
[[Category: Xanthomonas campestris]]
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[[Category: Chan, N.L.]]
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[[Category: Chan, N L.]]
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[[Category: Chang, J.L.]]
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[[Category: Chang, J L.]]
[[Category: Chen, Y.]]
[[Category: Chen, Y.]]
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[[Category: Chien, Y.L.]]
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[[Category: Chien, Y L.]]
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[[Category: Hu, N.T.]]
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[[Category: Hu, N T.]]
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[[Category: Huang, C.W.]]
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[[Category: Huang, C W.]]
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[[Category: Shiue, S.J.]]
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[[Category: Shiue, S J.]]
[[Category: alpha-beta sandwich]]
[[Category: alpha-beta sandwich]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:23:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:37 2008''

Revision as of 14:54, 21 February 2008


2d27, resolution 2.210Å

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Structure of the N-terminal domain of XpsE (crystal form I4122)

Overview

Secretion of fully folded extracellular proteins across the outer membrane of Gram-negative bacteria is mainly assisted by the ATP-dependent type II secretion system (T2SS). Depending on species, 12-15 proteins are usually required for the function of T2SS by forming a trans-envelope multiprotein secretion complex. Here we report crystal structures of an essential component of the Xanthomonas campestris T2SS, the 21-kDa N-terminal domain of cytosolic secretion ATPase XpsE (XpsEN), in two conformational states. By mediating interaction between XpsE and the cytoplasmic membrane protein XpsL, XpsEN anchors XpsE to the membrane-associated secretion complex to allow the coupling between ATP utilization and exoprotein secretion. The structure of XpsEN observed in crystal form P4(3)2(1)2 is composed of a 90-residue alpha/beta sandwich core domain capped by a 62-residue N-terminal helical region. The core domain exhibits structural similarity with the NifU-like domain, suggesting that XpsE(N) may be involved in the regulation of XpsE ATPase activity. Surprisingly, although a similar core domain structure was observed in crystal form I4(1)22, the N-terminal 36 residues of the helical region undergo a large structural rearrangement. Deletion analysis indicates that these residues are required for exoprotein secretion by mediating the XpsE/XpsL interaction. Site-directed mutagenesis study further suggests the more compact conformation observed in the P4(3)2(1)2 crystal likely represents the XpsL binding-competent state. Based on these findings, we speculate that XpsE might function in T2SS by cycling between two conformational states. As a closely related protein to XpsE, secretion ATPase PilB may function similarly in the type IV pilus assembly.

About this Structure

2D27 is a Single protein structure of sequence from Xanthomonas campestris. Full crystallographic information is available from OCA.

Reference

Structure and function of the XpsE N-terminal domain, an essential component of the Xanthomonas campestris type II secretion system., Chen Y, Shiue SJ, Huang CW, Chang JL, Chien YL, Hu NT, Chan NL, J Biol Chem. 2005 Dec 23;280(51):42356-63. Epub 2005 Sep 14. PMID:16162504

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