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2w49

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Revision as of 07:29, 21 August 2019

ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE

Structural highlights

2w49 is a 36 chain structure with sequence from Gallus gallus and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1tnq, 2aso, 1wua, 1o18, 2d1k, 1ncx, 1ew7, 2a5x, 2v52, 1j6z, 1npq, 1atn, 1ytz, 1s22, 1t44, 1zac, 2ff6, 1o1f, 2tma, 1blq, 1jc2, 1o19, 1o1e, 1p8z, 1o1c, 2vcp, 1o1g, 1vdi, 1qz6, 1avs, 1lcu, 2a42, 1top, 1ijj, 1tnx, 1m8q, 1o1a, 1rfq, 1uy5, 1ma9, 1rdw, 1o1b, 1o1d, 1ncy, 2a40, 1qz5, 1nwk, 1smg, 1sqk, 1tnp, 1pon, 1tnw, 2ff3, 1eqy, 1mvw, 2fxu, 2v51, 2d3e, 2asp, 1kxp, 1rgi, 1ncz, 1y64, 1alm, 1esv, 1h1v, 1skt, 2a3z, 1yv0, 1lot, 1vdj, 2asm, 2a41, 2vyp, 2w4u, 4tnc
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TPM1_RABIT] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. [TNNC2_CHICK] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. [TNNI2_CHICK] Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. [TNNT3_CHICK] Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. [ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: Isometric muscle contraction, where force is generated without muscle shortening, is a molecular traffic jam in which the number of actin-attached motors is maximized and all states of motor action are trapped with consequently high heterogeneity. This heterogeneity is a major limitation to deciphering myosin conformational changes in situ. METHODOLOGY: We used multivariate data analysis to group repeat segments in electron tomograms of isometrically contracting insect flight muscle, mechanically monitored, rapidly frozen, freeze substituted, and thin sectioned. Improved resolution reveals the helical arrangement of F-actin subunits in the thin filament enabling an atomic model to be built into the thin filament density independent of the myosin. Actin-myosin attachments can now be assigned as weak or strong by their motor domain orientation relative to actin. Myosin attachments were quantified everywhere along the thin filament including troponin. Strong binding myosin attachments are found on only four F-actin subunits, the "target zone", situated exactly midway between successive troponin complexes. They show an axial lever arm range of 77 degrees /12.9 nm. The lever arm azimuthal range of strong binding attachments has a highly skewed, 127 degrees range compared with X-ray crystallographic structures. Two types of weak actin attachments are described. One type, found exclusively in the target zone, appears to represent pre-working-stroke intermediates. The other, which contacts tropomyosin rather than actin, is positioned M-ward of the target zone, i.e. the position toward which thin filaments slide during shortening. CONCLUSION: We present a model for the weak to strong transition in the myosin ATPase cycle that incorporates azimuthal movements of the motor domain on actin. Stress/strain in the S2 domain may explain azimuthal lever arm changes in the strong binding attachments. The results support previous conclusions that the weak attachments preceding force generation are very different from strong binding attachments.

Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactions.,Wu S, Liu J, Reedy MC, Tregear RT, Winkler H, Franzini-Armstrong C, Sasaki H, Lucaveche C, Goldman YE, Reedy MK, Taylor KA PLoS One. 2010 Sep 9;5(9). pii: e12643. PMID:20844746^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wu S, Liu J, Reedy MC, Tregear RT, Winkler H, Franzini-Armstrong C, Sasaki H, Lucaveche C, Goldman YE, Reedy MK, Taylor KA. Electron tomography of cryofixed, isometrically contracting insect flight muscle reveals novel actin-myosin interactions. PLoS One. 2010 Sep 9;5(9). pii: e12643. PMID:20844746 doi:10.1371/journal.pone.0012643

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w49"

@@ Line 1: / Line 1: @@
 ==ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE==
-<StructureSection load='2w49' size='340' side='right' caption='[[2w49]], [[Resolution|resolution]] 35.00&Aring;' scene=''>
+<StructureSection load='2w49' size='340' side='right'caption='[[2w49]], [[Resolution|resolution]] 35.00&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2w49]] is a 36 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W49 FirstGlance]. <br>
@@ Line 14: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/2w49_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w4/2w49_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 31: @@
 ==See Also==
+*[[Actin 3D structures|Actin 3D structures]]
 *[[Tropomyosin|Tropomyosin]]
+*[[Troponin|Troponin]]
 == References ==
 <references/>
@@ Line 37: / Line 39: @@
 </StructureSection>
 [[Category: Gallus gallus]]
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
 [[Category: Franzini-Armstrong, C]]

2w49

From Proteopedia

Revision as of 07:29, 21 August 2019

ISOMETRICALLY CONTRACTING INSECT ASYNCHRONOUS FLIGHT MUSCLE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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