2d27
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2d27 |SIZE=350|CAPTION= <scene name='initialview01'>2d27</scene>, resolution 2.210Å | |PDB= 2d27 |SIZE=350|CAPTION= <scene name='initialview01'>2d27</scene>, resolution 2.210Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= xpsE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=339 Xanthomonas campestris]) | |GENE= xpsE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=339 Xanthomonas campestris]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2d28|2D28]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d27 OCA], [http://www.ebi.ac.uk/pdbsum/2d27 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d27 RCSB]</span> | ||
}} | }} | ||
| Line 31: | Line 34: | ||
[[Category: alpha-beta sandwich]] | [[Category: alpha-beta sandwich]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:20 2008'' |
Revision as of 23:29, 30 March 2008
| |||||||
| , resolution 2.210Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | xpsE (Xanthomonas campestris) | ||||||
| Related: | 2D28
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Mon Mar 31 02:29:20 2008
