From Proteopedia
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| - | [[Image:1mz0.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1mz0| PDB=1mz0 | SCENE= }} | | {{STRUCTURE_1mz0| PDB=1mz0 | SCENE= }} |
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| - | '''STRUCTURE OF MYOGLOBIN MB-YQR 316 ns AFTER PHOTOLYSIS OF CARBON MONOXIDE SOLVED FROM LAUE DATA AT RT.'''
| + | ===STRUCTURE OF MYOGLOBIN MB-YQR 316 ns AFTER PHOTOLYSIS OF CARBON MONOXIDE SOLVED FROM LAUE DATA AT RT.=== |
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| - | ==Overview==
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| - | Although conformational changes are essential for the function of proteins, little is known about their structural dynamics at atomic level resolution. Myoglobin (Mb) is the paradigm to investigate conformational dynamics because it is a simple globular heme protein displaying a photosensitivity of the iron-ligand bond. Upon laser photodissociation of carboxymyoglobin Mb a nonequilibrium population of protein structures is generated that relaxes over a broad time range extending from picoseconds to milliseconds. This process is associated with migration of the ligand to cavities in the matrix and with a reduction in the geminate rebinding rate by several orders of magnitude. Here we report nanosecond time-resolved Laue diffraction data to 1.55-A resolution on a Mb mutant, which depicts the sequence of structural events associated with this extended relaxation. Motions of the distal E-helix, including the mutated residue Gln-64(E7), and of the CD-turn are found to lag significantly (100-300 ns) behind local rearrangements around the heme such as heme tilting, iron motion out of the heme plane, and swinging of the mutated residue Tyr-29(B10), all of which occur promptly (< or =3 ns). Over the same delayed time range, CO is observed to migrate from a cavity distal to the heme known to bind xenon (called Xe4) to another such cavity proximal to the heme (Xe1). We propose that the extended relaxation of the globin moiety reflects reequilibration among conformational substates known to play an essential role in controlling protein function.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12847289}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12847289 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12847289}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Oxygen storage]] | | [[Category: Oxygen storage]] |
| | [[Category: Respiratory protein]] | | [[Category: Respiratory protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:53:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:40:00 2008'' |
Revision as of 09:40, 10 July 2008
Template:STRUCTURE 1mz0
STRUCTURE OF MYOGLOBIN MB-YQR 316 ns AFTER PHOTOLYSIS OF CARBON MONOXIDE SOLVED FROM LAUE DATA AT RT.
Template:ABSTRACT PUBMED 12847289
About this Structure
1MZ0 is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography., Bourgeois D, Vallone B, Schotte F, Arcovito A, Miele AE, Sciara G, Wulff M, Anfinrud P, Brunori M, Proc Natl Acad Sci U S A. 2003 Jul 22;100(15):8704-9. Epub 2003 Jul 7. PMID:12847289
Page seeded by OCA on Thu Jul 10 12:40:00 2008
