2bl0
From Proteopedia
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|PDB= 2bl0 |SIZE=350|CAPTION= <scene name='initialview01'>2bl0</scene>, resolution 1.75Å | |PDB= 2bl0 |SIZE=350|CAPTION= <scene name='initialview01'>2bl0</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+C'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+C'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bl0 OCA], [http://www.ebi.ac.uk/pdbsum/2bl0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bl0 RCSB]</span> | ||
}} | }} | ||
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==Reference== | ==Reference== | ||
Structural evidence for non-canonical binding of Ca2+ to a canonical EF-hand of a conventional myosin., Debreczeni JE, Farkas L, Harmat V, Hetenyi C, Hajdu I, Zavodszky P, Kohama K, Nyitray L, J Biol Chem. 2005 Dec 16;280(50):41458-64. Epub 2005 Oct 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16227209 16227209] | Structural evidence for non-canonical binding of Ca2+ to a canonical EF-hand of a conventional myosin., Debreczeni JE, Farkas L, Harmat V, Hetenyi C, Hajdu I, Zavodszky P, Kohama K, Nyitray L, J Biol Chem. 2005 Dec 16;280(50):41458-64. Epub 2005 Oct 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16227209 16227209] | ||
| + | [[Category: Myosin ATPase]] | ||
[[Category: Physarum polycephalum]] | [[Category: Physarum polycephalum]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Transferred entry: 3 6.4 1]] | ||
[[Category: Debreczeni, J E.]] | [[Category: Debreczeni, J E.]] | ||
[[Category: Farkas, L.]] | [[Category: Farkas, L.]] | ||
[[Category: Harmat, V.]] | [[Category: Harmat, V.]] | ||
[[Category: Nyitray, L.]] | [[Category: Nyitray, L.]] | ||
| - | [[Category: CA]] | ||
[[Category: ef-hand]] | [[Category: ef-hand]] | ||
[[Category: muscle protein]] | [[Category: muscle protein]] | ||
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[[Category: slime mould]] | [[Category: slime mould]] | ||
| - | ''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 02:07:59 2008'' |
Revision as of 23:08, 30 March 2008
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| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Myosin ATPase, with EC number 3.6.4.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHYSARUM POLYCEPHALUM MYOSIN II REGULATORY DOMAIN
Overview
We have previously identified a single inhibitory Ca2+-binding site in the first EF-hand of the essential light chain of Physarum conventional myosin (Farkas, L., Malnasi-Csizmadia, A., Nakamura, A., Kohama, K., and Nyitray, L. (2003) J. Biol. Chem. 278, 27399-27405). As a general rule, conformation of the EF-hand-containing domains in the calmodulin family is "closed" in the absence and "open" in the presence of bound cations; a notable exception is the unusual Ca2+-bound closed domain in the essential light chain of the Ca2+-activated scallop muscle myosin. Here we have reported the 1.8 A resolution structure of the regulatory domain (RD) of Physarum myosin II in which Ca2+ is bound to a canonical EF-hand that is also in a closed state. The 12th position of the EF-hand loop, which normally provides a bidentate ligand for Ca2+ in the open state, is too far in the structure to participate in coordination of the ion. The structure includes a second Ca2+ that only mediates crystal contacts. To reveal the mechanism behind the regulatory effect of Ca2+, we compared conformational flexibilities of the liganded and unliganded RD. Our working hypothesis, i.e. the modulatory effect of Ca2+ on conformational flexibility of RD, is in line with the observed suppression of hydrogen-deuterium exchange rate in the Ca2+-bound form, as well as with results of molecular dynamics calculations. Based on this evidence, we concluded that Ca2+-induced change in structural dynamics of RD is a major factor in Ca2+-mediated regulation of Physarum myosin II activity.
About this Structure
2BL0 is a Protein complex structure of sequences from Physarum polycephalum. Full crystallographic information is available from OCA.
Reference
Structural evidence for non-canonical binding of Ca2+ to a canonical EF-hand of a conventional myosin., Debreczeni JE, Farkas L, Harmat V, Hetenyi C, Hajdu I, Zavodszky P, Kohama K, Nyitray L, J Biol Chem. 2005 Dec 16;280(50):41458-64. Epub 2005 Oct 13. PMID:16227209
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