2ekv
From Proteopedia
(New page: 200px<br /><applet load="2ekv" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ekv" /> ''''''<br /> ==About this Structure== is a [h...) |
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[[Image:2ekv.jpg|left|200px]]<br /><applet load="2ekv" size="350" color="white" frame="true" align="right" spinBox="true" | [[Image:2ekv.jpg|left|200px]]<br /><applet load="2ekv" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2ekv" /> | + | caption="2ekv, resolution 3.4Å" /> |
| - | ''''''<br /> | + | '''The crystal structure of rigor like squid myosin S1 in the absence of nucleotide'''<br /> |
| + | |||
| + | ==Overview== | ||
| + | Unlike processive cellular motors such as myosin V, whose structure has, recently been determined in a "rigor-like" conformation, myosin II from, contracting muscle filaments necessarily spends most of its time detached, from actin. By using squid and sea scallop sources, however, we have now, obtained similar rigor-like atomic structures for muscle myosin heads, (S1). The significance of the hallmark closed actin-binding cleft in these, crystal structures is supported here by actin/S1-binding studies. These, structures reveal how different duty ratios, and hence cellular functions, of the myosin isoforms may be accounted for, in part, on the basis of, detailed differences in interdomain contacts. Moreover, the rigor-like, position of switch II turns out to be unique for myosin V. The overall, arrangements of subdomains in the motor are relatively conserved in each, of the known contractile states, and we explore qualitatively the, energetics of these states. | ||
==About this Structure== | ==About this Structure== | ||
| - | + | 2EKV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Loligo_plei Loligo plei] and [http://en.wikipedia.org/wiki/Todarodes_pacificus Todarodes pacificus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Residue+C+160'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EKV OCA]. | |
| + | |||
| + | ==Reference== | ||
| + | Rigor-like Structures from Muscle Myosins Reveal Key Mechanical Elements in the Transduction Pathways of This Allosteric Motor., Yang Y, Gourinath S, Kovacs M, Nyitray L, Reutzel R, Himmel DM, O'neall-Hennessey E, Reshetnikova L, Szent-Gyorgyi AG, Brown JH, Cohen C, Structure. 2007 May;15(5):553-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17502101 17502101] | ||
| + | [[Category: Loligo plei]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| + | [[Category: Todarodes pacificus]] | ||
| + | [[Category: Cohen, C.]] | ||
| + | [[Category: Neall-Hennessey, E.O.]] | ||
| + | [[Category: Reshetnikova, L.]] | ||
| + | [[Category: Yang, Y.]] | ||
| + | [[Category: CA]] | ||
| + | [[Category: contractile protein]] | ||
| + | [[Category: myosin s1]] | ||
| + | [[Category: nucleotide free]] | ||
| + | [[Category: rigor-like]] | ||
| + | [[Category: squid]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 6 17:21:53 2008'' |
Revision as of 15:21, 6 February 2008
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The crystal structure of rigor like squid myosin S1 in the absence of nucleotide
Overview
Unlike processive cellular motors such as myosin V, whose structure has, recently been determined in a "rigor-like" conformation, myosin II from, contracting muscle filaments necessarily spends most of its time detached, from actin. By using squid and sea scallop sources, however, we have now, obtained similar rigor-like atomic structures for muscle myosin heads, (S1). The significance of the hallmark closed actin-binding cleft in these, crystal structures is supported here by actin/S1-binding studies. These, structures reveal how different duty ratios, and hence cellular functions, of the myosin isoforms may be accounted for, in part, on the basis of, detailed differences in interdomain contacts. Moreover, the rigor-like, position of switch II turns out to be unique for myosin V. The overall, arrangements of subdomains in the motor are relatively conserved in each, of the known contractile states, and we explore qualitatively the, energetics of these states.
About this Structure
2EKV is a Protein complex structure of sequences from Loligo plei and Todarodes pacificus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Rigor-like Structures from Muscle Myosins Reveal Key Mechanical Elements in the Transduction Pathways of This Allosteric Motor., Yang Y, Gourinath S, Kovacs M, Nyitray L, Reutzel R, Himmel DM, O'neall-Hennessey E, Reshetnikova L, Szent-Gyorgyi AG, Brown JH, Cohen C, Structure. 2007 May;15(5):553-64. PMID:17502101
Page seeded by OCA on Wed Feb 6 17:21:53 2008
