1dxc
From Proteopedia
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|PDB= 1dxc |SIZE=350|CAPTION= <scene name='initialview01'>1dxc</scene>, resolution 1.4Å | |PDB= 1dxc |SIZE=350|CAPTION= <scene name='initialview01'>1dxc</scene>, resolution 1.4Å | ||
|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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dxc OCA], [http://www.ebi.ac.uk/pdbsum/1dxc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dxc RCSB]</span> | ||
}} | }} | ||
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[[Category: Travaglini-Allocatelli, C.]] | [[Category: Travaglini-Allocatelli, C.]] | ||
[[Category: Vallone, B.]] | [[Category: Vallone, B.]] | ||
| - | [[Category: CMO]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: SO4]] | ||
[[Category: co complex]] | [[Category: co complex]] | ||
[[Category: oxygen storage]] | [[Category: oxygen storage]] | ||
[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''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 19:50:38 2008'' |
Revision as of 16:50, 30 March 2008
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| , resolution 1.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CO COMPLEX OF MYOGLOBIN MB-YQR AT 100K
Overview
We determined the structure of the photolytic intermediate of a sperm whale myoglobin (Mb) mutant called Mb-YQR [Leu-(B10)-->Tyr; His(E7)-->Gln; Thr(E10)-->Arg] to 1.4-A resolution by ultra-low temperature (20 K) x-ray diffraction. Starting with the CO complex, illumination leads to photolysis of the Fe-CO bond, and migration of the photolyzed carbon monoxide (CO*) to a niche in the protein 8.1 A from the heme iron; this cavity corresponds to that hosting an atom of Xe when the crystal is equilibrated with xenon gas at 7 atmospheres [Tilton, R. F., Jr., Kuntz, I. D. & Petsko, G. A. (1984) Biochemistry 23, 2849-2857]. The site occupied by CO* corresponds to that predicted by molecular dynamics simulations previously carried out to account for the NO geminate rebinding of Mb-YQR observed in laser photolysis experiments at room temperature. This secondary docking site differs from the primary docking site identified by previous crystallographic studies on the photolyzed intermediate of wild-type sperm whale Mb performed at cryogenic temperatures [Teng et al. (1994) Nat. Struct. Biol. 1, 701-705] and room temperature [Srajer et al. (1996) Science 274, 1726-1729]. Our experiment shows that the pathway of a small molecule in its trajectory through a protein may be modified by site-directed mutagenesis, and that migration within the protein matrix to the active site involves a limited number of pre-existing cavities identified in the interior space of the protein.
About this Structure
1DXC is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin., Brunori M, Vallone B, Cutruzzola F, Travaglini-Allocatelli C, Berendzen J, Chu K, Sweet RM, Schlichting I, Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2058-63. PMID:10681426
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