2b8i
From Proteopedia
(New page: 200px<br /><applet load="2b8i" size="350" color="white" frame="true" align="right" spinBox="true" caption="2b8i, resolution 1.8Å" /> '''Crystal Structure and...) |
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==Overview== | ==Overview== | ||
| - | PAS factor is a novel putative bacterial secretion factor thought to | + | PAS factor is a novel putative bacterial secretion factor thought to induce secretion of periplasmic proteins. We solved the crystal structure of PAS factor from Vibrio vulnificus at 1.8A resolution and found it to be comprised of five alpha helices that form an antiparallel bundle with an up-and-down topology, and to adopt the saposin-fold characteristic of a family of proteins that bind to membranes and lipids. PAS factor lacks the disulfide bridge characteristic of mammalian saposin-fold proteins; in fact, it shows no sequence homology with mammalian proteins. Nevertheless, the molecular architectures are similar, and the shared propensity for membrane interaction suggests strongly that PAS factor is another member of the saposin-fold family. Analysis of the CD spectra showed that PAS factor binds to membranes directly, while measurement of calcein dye leakage showed that PAS factor interacts strongly with liposomes composed of anionic phospholipids, making them leaky, but binds very weakly with liposomes composed of zwitterionic phospholipids. Moreover, by analyzing tryptophan fluorescence emission from four single-tryptophan mutants (V10W, T22W, F35W, and L70W), we identified the putative phospholipid-binding site of PAS factor. The resultant membrane destabilization likely mediates secretion of periplasmic proteins required for the in vivo survival and pathogenesis of V.vulnificus. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Vibrio vulnificus]] | [[Category: Vibrio vulnificus]] | ||
| - | [[Category: Eom, S | + | [[Category: Eom, S H.]] |
| - | [[Category: Im, Y | + | [[Category: Im, Y J.]] |
| - | [[Category: Kang, G | + | [[Category: Kang, G B.]] |
| - | [[Category: Kim, J | + | [[Category: Kim, J I.]] |
| - | [[Category: Kim, M | + | [[Category: Kim, M K.]] |
| - | [[Category: Kim, S | + | [[Category: Kim, S Y.]] |
| - | [[Category: Kim, Y | + | [[Category: Kim, Y R.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J H.]] |
| - | [[Category: Rhee, J | + | [[Category: Rhee, J H.]] |
| - | [[Category: Rho, S | + | [[Category: Rho, S H.]] |
| - | [[Category: Yang, S | + | [[Category: Yang, S T.]] |
[[Category: four helix bundle]] | [[Category: four helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:11 2008'' |
Revision as of 14:35, 21 February 2008
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Crystal Structure and Functional Studies Reveal that PAS Factor from Vibrio vulnificus is a Novel Member of the Saposin-Fold Family
Overview
PAS factor is a novel putative bacterial secretion factor thought to induce secretion of periplasmic proteins. We solved the crystal structure of PAS factor from Vibrio vulnificus at 1.8A resolution and found it to be comprised of five alpha helices that form an antiparallel bundle with an up-and-down topology, and to adopt the saposin-fold characteristic of a family of proteins that bind to membranes and lipids. PAS factor lacks the disulfide bridge characteristic of mammalian saposin-fold proteins; in fact, it shows no sequence homology with mammalian proteins. Nevertheless, the molecular architectures are similar, and the shared propensity for membrane interaction suggests strongly that PAS factor is another member of the saposin-fold family. Analysis of the CD spectra showed that PAS factor binds to membranes directly, while measurement of calcein dye leakage showed that PAS factor interacts strongly with liposomes composed of anionic phospholipids, making them leaky, but binds very weakly with liposomes composed of zwitterionic phospholipids. Moreover, by analyzing tryptophan fluorescence emission from four single-tryptophan mutants (V10W, T22W, F35W, and L70W), we identified the putative phospholipid-binding site of PAS factor. The resultant membrane destabilization likely mediates secretion of periplasmic proteins required for the in vivo survival and pathogenesis of V.vulnificus.
About this Structure
2B8I is a Single protein structure of sequence from Vibrio vulnificus. Full crystallographic information is available from OCA.
Reference
Crystal structure and functional studies reveal that PAS factor from Vibrio vulnificus is a novel member of the saposin-fold family., Lee JH, Yang ST, Rho SH, Im YJ, Kim SY, Kim YR, Kim MK, Kang GB, Kim JI, Rhee JH, Eom SH, J Mol Biol. 2006 Jan 20;355(3):491-500. Epub 2005 Nov 14. PMID:16318855
Page seeded by OCA on Thu Feb 21 16:35:11 2008
Categories: Single protein | Vibrio vulnificus | Eom, S H. | Im, Y J. | Kang, G B. | Kim, J I. | Kim, M K. | Kim, S Y. | Kim, Y R. | Lee, J H. | Rhee, J H. | Rho, S H. | Yang, S T. | Four helix bundle
