1txe: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1txe.gif|left|200px]] | [[Image:1txe.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1txe", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1txe| PDB=1txe | SCENE= }} | |||
}} | |||
'''Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus''' | '''Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus''' | ||
| Line 31: | Line 28: | ||
[[Category: Moeglich, A.]] | [[Category: Moeglich, A.]] | ||
[[Category: SPINE, Structural Proteomics in Europe.]] | [[Category: SPINE, Structural Proteomics in Europe.]] | ||
[[Category: | [[Category: Open-faced beta-sandwich]] | ||
[[Category: | [[Category: Spine]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: | [[Category: Structural proteomics in europe]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:12:15 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 08:12, 13 April 2008
Solution structure of the active-centre mutant Ile14Ala of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus
OverviewOverview
High-pressure NMR experiments performed on the histidine-containing phosphocarrier protein (HPr) from Staphylococcus carnosus have shown that residue Ile14, which is located in the active-centre loop, exhibits a peculiarly small pressure response. In contrast, the rest of the loop shows strong pressure effects as is expected for typical protein interaction sites. To elucidate the structural role of this residue, the mutant protein HPr(I14A), in which Ile14 is replaced by Ala, was produced and studied by solution NMR spectroscopy. On the basis of 1406 structural restraints including 20 directly detected hydrogen bonds, 49 1H(N)-15N, and 25 1H(N)-1Halpha residual dipolar couplings, a well resolved three-dimensional structure could be determined. The overall fold of the protein is not influenced by the mutation but characteristic conformational changes are introduced into the active-centre loop. They lead to a displacement of the ring system of His15 and a distortion of the N-terminus of the first helix, which supports the histidine ring. In addition, the C-terminal helix is bent because the side chain of Leu86 located at the end of this helix partly fills the hydrophobic cavity created by the mutation. Xenon, which is known to occupy hydrophobic cavities, causes a partial reversal of the mutation-induced structural effects. The observed structural changes explain the reduced phosphocarrier activity of the mutant and agree well with the earlier suggestion that Ile14 represents an anchoring point stabilizing the active-centre loop in its correct conformation.
About this StructureAbout this Structure
1TXE is a Single protein structure of sequence from Staphylococcus carnosus. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus., Moglich A, Koch B, Gronwald W, Hengstenberg W, Brunner E, Kalbitzer HR, Eur J Biochem. 2004 Dec;271(23-24):4815-24. PMID:15606769 Page seeded by OCA on Sun Apr 13 08:12:15 2008