2fxm: Difference between revisions
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|PDB= 2fxm |SIZE=350|CAPTION= <scene name='initialview01'>2fxm</scene>, resolution 2.70Å | |PDB= 2fxm |SIZE=350|CAPTION= <scene name='initialview01'>2fxm</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HG:MERCURY (II) ION'>HG</scene> | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= HSBMHC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= HSBMHC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2fxo|2FXO]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxm OCA], [http://www.ebi.ac.uk/pdbsum/2fxm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fxm RCSB]</span> | |||
}} | }} | ||
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[[Category: Thoma, N H.]] | [[Category: Thoma, N H.]] | ||
[[Category: Wray, J S.]] | [[Category: Wray, J S.]] | ||
[[Category: coiled coil (dimeric]] | [[Category: coiled coil (dimeric]] | ||
[[Category: familial hypertrophic cardiomyopathy]] | [[Category: familial hypertrophic cardiomyopathy]] | ||
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[[Category: thick filament]] | [[Category: thick filament]] | ||
''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 03:09:01 2008'' | ||
Revision as of 03:09, 31 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | HSBMHC (Homo sapiens) | ||||||
| Related: | 2FXO
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the human beta-myosin S2 fragment
OverviewOverview
Myosin II is the major component of the muscle thick filament. It consists of two N-terminal S1 subfragments ("heads") connected to a long dimeric coiled-coil rod. The rod is in itself twofold symmetric, but in the filament, the two heads point away from the filament surface and are therefore not equivalent. This breaking of symmetry requires the initial section of the rod, subfragment 2 (S2), to be relatively flexible. S2 is an important functional element, involved in various mechanisms by which the activity of smooth and striated muscle is regulated. We have determined crystal structures of the 126 N-terminal residues of S2 from human cardiac beta-myosin II (S2-Delta), of both WT and the disease-associated E924K mutant. S2-Delta is a straight parallel dimeric coiled coil, but the N terminus of one chain is disordered in WT-S2-Delta due to crystal contacts, indicative of unstable local structure. Bulky noncanonical side chains pack into a/d positions of S2-Delta's N terminus, leading to defined local asymmetry and axial stagger, which could induce nonequivalence of the S1 subfragments. Additionally, S2 possesses a conserved charge distribution with three prominent rings of negative potential within S2-Delta, the first of which may provide a binding interface for the "blocked head" of smooth muscle myosin in the OFF state. The observation that many disease-associated mutations affect the second negatively charged ring further suggests that charge interactions play an important role in regulation of cardiac muscle activity through myosin-binding protein C.
About this StructureAbout this Structure
2FXM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment., Blankenfeldt W, Thoma NH, Wray JS, Gautel M, Schlichting I, Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17713-7. Epub 2006 Nov 9. PMID:17095604
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