1fu0
From Proteopedia
(New page: 200px<br /><applet load="1fu0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fu0, resolution 1.90Å" /> '''CRYSTAL STRUCTURE AN...) |
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| - | [[Image:1fu0.jpg|left|200px]]<br /><applet load="1fu0" size=" | + | [[Image:1fu0.jpg|left|200px]]<br /><applet load="1fu0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fu0, resolution 1.90Å" /> | caption="1fu0, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF THE PHOSPHO-SERINE 46 HPR FROM ENTEROCOCCUS FAECALIS'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF THE PHOSPHO-SERINE 46 HPR FROM ENTEROCOCCUS FAECALIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The histidine-containing phosphocarrier protein HPr is a central component | + | The histidine-containing phosphocarrier protein HPr is a central component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), which transfers metabolic carbohydrates across the cell membrane in many bacterial species. In Gram-positive bacteria, phosphorylation of HPr at conserved serine 46 (P-Ser-HPr) plays several regulatory roles within the cell; the major regulatory effect of P-Ser-HPr is its inability to act as a phosphocarrier substrate in the enzyme I reaction of the PTS. In order to investigate the structural nature of HPr regulation by phosphorylation at Ser46, the structure of the P-Ser-HPr from the Gram- positive bacterium Enterococcus faecalis has been determined. X-ray diffraction analysis of P-Ser-HPr crystals provided 10,043 unique reflections, with a 95.1 % completeness of data to 1.9 A resolution. The structure was solved using molecular replacement, with two P-Ser-HPr molecules present in the asymmetric unit. The final R-value and R(Free) are 0.178 and 0.239, respectively. The overall tertiary structure of P-Ser-HPr is that of other HPr structures. However the active site in both P-Ser-HPr molecules was found to be in the "open" conformation. Ala16 of both molecules were observed to be in a state of torsional strain, similar to that seen in the structure of the native HPr from E. faecalis. Regulatory phosphorylation at Ser46 does not induce large structural changes to the HPr molecule. The B-helix was observed to be slightly lengthened as a result of Ser46 phosphorylation. Also, the water mediated Met51-His15 interaction is maintained, again similar to that of the native E. faecalis HPr. The major structural, and thus regulatory, effect of phosphorylation at Ser46 is disruption of the hydrophobic interactions between EI and HPr, in particular the electrostatic repulsion between the phosphoryl group on Ser46 and Glu84 of EI and the prevention of a potential interaction of Met48 with a hydrophobic pocket of EI. |
==About this Structure== | ==About this Structure== | ||
| - | 1FU0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http:// | + | 1FU0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FU0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Audette, G | + | [[Category: Audette, G F.]] |
| - | [[Category: Delbaere, L | + | [[Category: Delbaere, L T.J.]] |
[[Category: Deutscher, J.]] | [[Category: Deutscher, J.]] | ||
[[Category: Engelmann, R.]] | [[Category: Engelmann, R.]] | ||
[[Category: Hayakawa, K.]] | [[Category: Hayakawa, K.]] | ||
[[Category: Hengstenberg, W.]] | [[Category: Hengstenberg, W.]] | ||
| - | [[Category: Quail, J | + | [[Category: Quail, J W.]] |
[[Category: phospho-serine hpr]] | [[Category: phospho-serine hpr]] | ||
[[Category: pts system]] | [[Category: pts system]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:40 2008'' |
Revision as of 10:42, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF THE PHOSPHO-SERINE 46 HPR FROM ENTEROCOCCUS FAECALIS
Overview
The histidine-containing phosphocarrier protein HPr is a central component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), which transfers metabolic carbohydrates across the cell membrane in many bacterial species. In Gram-positive bacteria, phosphorylation of HPr at conserved serine 46 (P-Ser-HPr) plays several regulatory roles within the cell; the major regulatory effect of P-Ser-HPr is its inability to act as a phosphocarrier substrate in the enzyme I reaction of the PTS. In order to investigate the structural nature of HPr regulation by phosphorylation at Ser46, the structure of the P-Ser-HPr from the Gram- positive bacterium Enterococcus faecalis has been determined. X-ray diffraction analysis of P-Ser-HPr crystals provided 10,043 unique reflections, with a 95.1 % completeness of data to 1.9 A resolution. The structure was solved using molecular replacement, with two P-Ser-HPr molecules present in the asymmetric unit. The final R-value and R(Free) are 0.178 and 0.239, respectively. The overall tertiary structure of P-Ser-HPr is that of other HPr structures. However the active site in both P-Ser-HPr molecules was found to be in the "open" conformation. Ala16 of both molecules were observed to be in a state of torsional strain, similar to that seen in the structure of the native HPr from E. faecalis. Regulatory phosphorylation at Ser46 does not induce large structural changes to the HPr molecule. The B-helix was observed to be slightly lengthened as a result of Ser46 phosphorylation. Also, the water mediated Met51-His15 interaction is maintained, again similar to that of the native E. faecalis HPr. The major structural, and thus regulatory, effect of phosphorylation at Ser46 is disruption of the hydrophobic interactions between EI and HPr, in particular the electrostatic repulsion between the phosphoryl group on Ser46 and Glu84 of EI and the prevention of a potential interaction of Met48 with a hydrophobic pocket of EI.
About this Structure
1FU0 is a Single protein structure of sequence from Enterococcus faecalis. Full crystallographic information is available from OCA.
Reference
The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis., Audette GF, Engelmann R, Hengstenberg W, Deutscher J, Hayakawa K, Quail JW, Delbaere LT, J Mol Biol. 2000 Nov 3;303(4):545-53. PMID:11054290
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