1myf
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1myf.gif|left|200px]] | [[Image:1myf.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1myf", 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_1myf| PDB=1myf | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''SOLUTION STRUCTURE OF CARBONMONOXY MYOGLOBIN DETERMINED FROM NMR DISTANCE AND CHEMICAL SHIFT CONSTRAINTS''' | '''SOLUTION STRUCTURE OF CARBONMONOXY MYOGLOBIN DETERMINED FROM NMR DISTANCE AND CHEMICAL SHIFT CONSTRAINTS''' | ||
| Line 29: | Line 26: | ||
[[Category: Theriault, Y.]] | [[Category: Theriault, Y.]] | ||
[[Category: Wright, P E.]] | [[Category: Wright, P E.]] | ||
| - | [[Category: | + | [[Category: Oxygen transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:52:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:52, 2 May 2008
SOLUTION STRUCTURE OF CARBONMONOXY MYOGLOBIN DETERMINED FROM NMR DISTANCE AND CHEMICAL SHIFT CONSTRAINTS
Overview
Solution NMR structures for sperm whale carbonmonoxy myoglobin have been calculated using 1301 distance restraints determined from nuclear Overhauser enhancement (NOE) measurements on 15N-labeled protein and chemical shift calculations for 385 protons. Starting structures included four crystal forms of myoglobin and 12 structures generated by metric matrix distance geometry. Refinements were also carried out using distance restraints alone. In general, the solution conformations are very close to the crystal structures, although the crystal structures are not consistent with some of the observed NOE connectivities. The solution structures are about as far apart from each other (as measured by backbone root-mean-square deviations) as they are from the crystal conformation. Inclusion of chemical shift restraints both tightened the spread of computed structures (especially in the heme pocket region) and led to structures that were closer to the X-ray conformation. The disposition of the side-chains near the heme group could in many cases be determined with considerable confidence, suggesting that a chemical shift analysis may be a useful adjunct to other sources of structural information available from NMR. In particular, this evidence suggests that the distal histidine residue is slightly displaced from the crystal conformation, but still inside the heme pocket at pH 5.6, that the side-chain of Leu89 is in contact with the heme ring but is probably disordered, and that the heme pocket where ligands bind is virtually identical in solution and in the crystal forms.
About this Structure
1MYF is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints., Osapay K, Theriault Y, Wright PE, Case DA, J Mol Biol. 1994 Nov 25;244(2):183-97. PMID:7966330 Page seeded by OCA on Sat May 3 01:52:07 2008
