1dxc
From Proteopedia
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| - | [[Image:1dxc.gif|left|200px]] | + | [[Image:1dxc.gif|left|200px]] |
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| - | '''CO COMPLEX OF MYOGLOBIN MB-YQR AT 100K''' | + | {{Structure |
| + | |PDB= 1dxc |SIZE=350|CAPTION= <scene name='initialview01'>1dxc</scene>, resolution 1.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CMO:CARBON MONOXIDE'>CMO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CO COMPLEX OF MYOGLOBIN MB-YQR AT 100K''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DXC is a [ | + | 1DXC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DXC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10681426 10681426] |
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:45:55 2008'' |
Revision as of 08:45, 20 March 2008
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| , resolution 1.4Å | |||||||
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| Ligands: | , and | ||||||
| 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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