1myf | pdb_00001myf

SOLUTION STRUCTURE OF CARBONMONOXY MYOGLOBIN DETERMINED FROM NMR DISTANCE AND CHEMICAL SHIFT CONSTRAINTS

spinqualitylabelsall models 1myf Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1myf is a 1 chain structure with sequence from Physeter catodon. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, models Ligands: CMO, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myoglobin 3D structures

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