1fi3
From Proteopedia
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|PDB= 1fi3 |SIZE=350|CAPTION= <scene name='initialview01'>1fi3</scene> | |PDB= 1fi3 |SIZE=350|CAPTION= <scene name='initialview01'>1fi3</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEC:HEME C'>HEC</scene> | + | |LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1cch|1CCH]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fi3 OCA], [http://www.ebi.ac.uk/pdbsum/1fi3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fi3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Miller, G T.]] | [[Category: Miller, G T.]] | ||
[[Category: Timkovich, R.]] | [[Category: Timkovich, R.]] | ||
| - | [[Category: HEC]] | ||
[[Category: c-551 family]] | [[Category: c-551 family]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:23:19 2008'' |
Revision as of 17:23, 30 March 2008
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| Ligands: | |||||||
| Related: | 1CCH
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE M61H MUTANT OF PSEUDOMONAS STUTZERI SUBSTRAIN ZOBELL FERROCYTOCHROME C-551
Overview
The gene encoding for bacterial cytochrome c-551 from Pseudomonas stutzeri substrain ZoBell has been mutated to convert the invariant sixth ligand methionine residue into histidine, creating the site-specific mutant M61H. Proton NMR resonance assignments were made for all main-chain and most-side chain protons in the diamagnetic, reduced form at pH 9.2 and 333 K by two-dimensional NMR techniques. Distance constraints (1074) were determined from nuclear Overhauser enhancements and main-chain torsion-angle constraints (72) from scalar coupling estimates. Solution conformations for the protein were computed by the simulated annealing approach. For 28 computed structures, the root mean squared displacement from the average structure excluding the terminal residues 1, 2, 81, and 82 was 0.52 A (sigma = 0.096) for backbone atoms and 0.90 A (sigma = 0.122) for all heavy atoms. The global folding of the mutant protein is the same as for wild type. The biggest changes are localized in a peptide span over residues 60-65. The most striking behavior of the mutant protein is that at room temperature and neutral pH it exists in a state similar to the molten globular state that has been described for several proteins under mild denaturing conditions, but the mutant converts to a more ordered state at high pH and temperature.
About this Structure
1FI3 is a Single protein structure of sequence from Pseudomonas stutzeri. Full crystallographic information is available from OCA.
Reference
Solution conformation of the Met 61 to His 61 mutant of Pseudomonas stutzeri ZoBell ferrocytochrome c-551., Miller GT, Hardman JK, Timkovich R, Biophys J. 2001 Jun;80(6):2928-34. PMID:11371465
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