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2bl0

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[[Image:2bl0.gif|left|200px]]<br /><applet load="2bl0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bl0.gif|left|200px]]
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caption="2bl0, resolution 1.75&Aring;" />
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'''PHYSARUM POLYCEPHALUM MYOSIN II REGULATORY DOMAIN'''<br />
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{{Structure
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|PDB= 2bl0 |SIZE=350|CAPTION= <scene name='initialview01'>2bl0</scene>, resolution 1.75&Aring;
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|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+C'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.4.1 Transferred entry: 3.6.4.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.32 3.6.1.32]
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|GENE=
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}}
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'''PHYSARUM POLYCEPHALUM MYOSIN II REGULATORY DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BL0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.4.1 Transferred entry: 3.6.4.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.32 3.6.1.32] Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+C'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BL0 OCA].
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2BL0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Physarum_polycephalum Physarum polycephalum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BL0 OCA].
==Reference==
==Reference==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16227209 16227209]
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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: Physarum polycephalum]]
[[Category: Physarum polycephalum]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: slime mould]]
[[Category: slime mould]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:03:19 2008''

Revision as of 14:03, 20 March 2008


PDB ID 2bl0

Drag the structure with the mouse to rotate
, resolution 1.75Å
Sites:
Ligands:
Activity: Transferred entry: 3.6.4.1, with EC number 3.6.1.32
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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