From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
Line 1: |
Line 1: |
- | [[Image:2d27.gif|left|200px]] | + | {{Seed}} |
| + | [[Image:2d27.png|left|200px]] |
| | | |
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_2d27| PDB=2d27 | SCENE= }} | | {{STRUCTURE_2d27| PDB=2d27 | SCENE= }} |
| | | |
- | '''Structure of the N-terminal domain of XpsE (crystal form I4122)'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16162504}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 16162504 is the PubMed ID number. |
| + | --> |
| + | {{ABSTRACT_PUBMED_16162504}} |
| | | |
| ==About this Structure== | | ==About this Structure== |
Line 30: |
Line 34: |
| [[Category: Shiue, S J.]] | | [[Category: Shiue, S J.]] |
| [[Category: Alpha-beta sandwich]] | | [[Category: Alpha-beta sandwich]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:33:52 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:37:16 2008'' |
Revision as of 16:37, 28 July 2008
Template:STRUCTURE 2d27
Structure of the N-terminal domain of XpsE (crystal form I4122)
Template:ABSTRACT PUBMED 16162504
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
Page seeded by OCA on Mon Jul 28 19:37:16 2008