1vrf
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(New page: 200px<br /> <applet load="1vrf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vrf" /> '''SOLUTION STRUCTURE OF COMPONENT IV GLYCERA ...)
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Revision as of 11:14, 8 November 2007
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SOLUTION STRUCTURE OF COMPONENT IV GLYCERA DIBRANCHIATA MONOMERIC HEMOGLOBIN-CO
Overview
The solution structure and backbone dynamics of the recombinant, ferrous, CO-ligated form of component IV monomeric hemoglobin from Glycera, dibranchiata (GMH4CO) have been characterized by NMR spectroscopy., Distance geometry and simulated annealing calculations utilizing a total, of 2550 distance and torsion angle constraints yielded an ensemble of 29, structures with an overall average backbone rmsd of 0.48 A from the, average structure. Differences between the solution structure and a, related crystal structure are confined to regions of lower precision in, either the NMR or X-ray structure, or in regions where the amino acid, sequences differ. 15N relaxation measurements at 76.0 and 60.8 MHz were, analyzed with an extended model-free approach, and revealed low-frequency, motions in the vicinity of the heme, concentrated in the F helix. Amide, proton protection factors were obtained from H-D amide exchange, measurements on 15N-labeled protein. Patterns in the backbone dynamics and, protection factors were shown to correlate with regions of heterogeneity, and disorder in the ensemble of NMR structures and with large, crystallographic B-factors in the X-ray structures. Surprisingly, while, the backbone atoms of the F helix have higher rmsds and larger measures of, dynamics on the microsecond to millisecond time scale than the other, helices, amide protection factors for residues in the F helix were, observed to be similar to those of the other helices. This contrasts with, H-D amide exchange measurements on sperm whale myoglobin which indicated, low protection for the F helix (S. N. Loh and B. F. Volkman, unpublished, results). These results for GMH4 suggest a model in which the F helix, undergoes collective motions as a relatively rigid hydrogen-bonded unit, possibly pivoting about a central position near residue Val87.
About this Structure
1VRF is a Single protein structure of sequence from Glycera dibranchiata with HEM and CMO as ligands. Full crystallographic information is available from OCA.
Reference
Solution structure and backbone dynamics of component IV Glycera dibranchiata monomeric hemoglobin-CO., Volkman BF, Alam SL, Satterlee JD, Markley JL, Biochemistry. 1998 Aug 4;37(31):10906-19. PMID:9692983
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