2r15

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(New page: 200px<br /><applet load="2r15" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r15, resolution 2.24&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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Sarcomeric filament proteins display extraordinary properties in terms of, protein length and mechanical elasticity, requiring specific anchoring and, assembly mechanisms. To establish the molecular basis of terminal filament, assembly, we have selected the sarcomeric M-band protein myomesin as a, prototypic filament model. The crystal structure of the myomesin, C-terminus, comprising a tandem array of two immunoglobulin (Ig) domains, My12 and My13, reveals a dimeric end-to-end filament of 14.3 nm length., Although the two domains share the same fold, an unexpected rearrangement, of one beta-strand reveals how they are evolved into unrelated functions, terminal filament assembly (My13) and filament propagation (My12). The two, domains are connected by a six-turn alpha-helix, of which two turns are, void of any interactions with other protein parts. Thus, the overall, structure of the assembled myomesin C-terminus resembles a three-body, beads-on-the-string model with potentially elastic properties. We predict, that the found My12-helix-My13 domain topology may provide a structural, template for the filament architecture of the entire C-terminal Ig domain, array My9-My13 of myomesin.
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Sarcomeric filament proteins display extraordinary properties in terms of protein length and mechanical elasticity, requiring specific anchoring and assembly mechanisms. To establish the molecular basis of terminal filament assembly, we have selected the sarcomeric M-band protein myomesin as a prototypic filament model. The crystal structure of the myomesin C-terminus, comprising a tandem array of two immunoglobulin (Ig) domains My12 and My13, reveals a dimeric end-to-end filament of 14.3 nm length. Although the two domains share the same fold, an unexpected rearrangement of one beta-strand reveals how they are evolved into unrelated functions, terminal filament assembly (My13) and filament propagation (My12). The two domains are connected by a six-turn alpha-helix, of which two turns are void of any interactions with other protein parts. Thus, the overall structure of the assembled myomesin C-terminus resembles a three-body beads-on-the-string model with potentially elastic properties. We predict that the found My12-helix-My13 domain topology may provide a structural template for the filament architecture of the entire C-terminal Ig domain array My9-My13 of myomesin.
==About this Structure==
==About this Structure==
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2R15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Gol Binding Site For Residue A 601'>AC1</scene>, <scene name='pdbsite=AC2:Gol Binding Site For Residue B 602'>AC2</scene> and <scene name='pdbsite=AC3:Gol Binding Site For Residue B 603'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R15 OCA].
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2R15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+A+601'>AC1</scene>, <scene name='pdbsite=AC2:Gol+Binding+Site+For+Residue+B+602'>AC2</scene> and <scene name='pdbsite=AC3:Gol+Binding+Site+For+Residue+B+603'>AC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R15 OCA].
==Reference==
==Reference==
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[[Category: thick filament]]
[[Category: thick filament]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:59:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:51 2008''

Revision as of 16:43, 21 February 2008


2r15, resolution 2.24Å

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Crystal structure of the myomesin domains 12 and 13

Overview

Sarcomeric filament proteins display extraordinary properties in terms of protein length and mechanical elasticity, requiring specific anchoring and assembly mechanisms. To establish the molecular basis of terminal filament assembly, we have selected the sarcomeric M-band protein myomesin as a prototypic filament model. The crystal structure of the myomesin C-terminus, comprising a tandem array of two immunoglobulin (Ig) domains My12 and My13, reveals a dimeric end-to-end filament of 14.3 nm length. Although the two domains share the same fold, an unexpected rearrangement of one beta-strand reveals how they are evolved into unrelated functions, terminal filament assembly (My13) and filament propagation (My12). The two domains are connected by a six-turn alpha-helix, of which two turns are void of any interactions with other protein parts. Thus, the overall structure of the assembled myomesin C-terminus resembles a three-body beads-on-the-string model with potentially elastic properties. We predict that the found My12-helix-My13 domain topology may provide a structural template for the filament architecture of the entire C-terminal Ig domain array My9-My13 of myomesin.

About this Structure

2R15 is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Sites: , and . Full crystallographic information is available from OCA.

Reference

Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin., Pinotsis N, Lange S, Perriard JC, Svergun DI, Wilmanns M, EMBO J. 2008 Jan 9;27(1):253-64. Epub 2007 Dec 6. PMID:18059477

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