1vrf
From Proteopedia
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|PDB= 1vrf |SIZE=350|CAPTION= <scene name='initialview01'>1vrf</scene> | |PDB= 1vrf |SIZE=350|CAPTION= <scene name='initialview01'>1vrf</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vrf OCA], [http://www.ebi.ac.uk/pdbsum/1vrf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vrf RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Satterlee, J D.]] | [[Category: Satterlee, J D.]] | ||
[[Category: Volkman, B F.]] | [[Category: Volkman, B F.]] | ||
| - | [[Category: CMO]] | ||
| - | [[Category: HEM]] | ||
[[Category: globin]] | [[Category: globin]] | ||
[[Category: heme protein]] | [[Category: heme protein]] | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:27:41 2008'' |
Revision as of 21:27, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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