1neh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1neh.gif|left|200px]] | [[Image:1neh.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1neh", 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_1neh| PDB=1neh | SCENE= }} | |||
}} | |||
'''HIGH POTENTIAL IRON-SULFUR PROTEIN''' | '''HIGH POTENTIAL IRON-SULFUR PROTEIN''' | ||
| Line 31: | Line 28: | ||
[[Category: Sompornpisut, P.]] | [[Category: Sompornpisut, P.]] | ||
[[Category: 4fe-4]] | [[Category: 4fe-4]] | ||
[[Category: | [[Category: Electron transport]] | ||
[[Category: | [[Category: Iron-sulfur]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:26:05 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 02:26, 3 May 2008
HIGH POTENTIAL IRON-SULFUR PROTEIN
OverviewOverview
The NMR solution structure of the oxidized HiPIP from Chromatium vinosum has been solved. Despite the fact that the protein is paramagnetic, 85% of the 1H and 80% of the 15N signals have been assigned. Through 1537 NOEs, out of which 1142 were found to be relevant for the structure determination, a family of structures has been obtained by distance geometry calculations. These structures have then been subjected to restrained energy minimization (REM) and restrained molecular dynamics (RMD) calculations in vacuum. Finally, the mean structure of the RMD family has been treated through RMD in water. The RMSD values for the backbone and heavy atoms within the RMD family are 0.57 +/- 0.14 and 1.08 +/- 0.16 A, respectively. These values together with other parameters indicate that the structure is of good quality and as good as the structure of the reduced protein. The RMDw structures of the reduced and oxidized proteins are different beyond the experimental indetermination. The set of constraints for the reduced and oxidized forms have been used to treat the available X-ray structure by RMD in water. The two structures generated in this way are quite similar to their respective solution structures, thus confirming that the experimental constraints are capable of yielding two different structures from the same starting structural model. This is the first time that independently determined solution structures of two redox states of a paramagnetic protein are available. Differences between them and the X-ray structure are discussed.
About this StructureAbout this Structure
1NEH is a Single protein structure of sequence from Allochromatium vinosum. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species., Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P, Biochemistry. 1995 Aug 8;34(31):9851-8. PMID:7632685 Page seeded by OCA on Sat May 3 02:26:05 2008