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1oe9

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Revision as of 07:12, 25 August 2021

Crystal structure of Myosin V motor with essential light chain-nucleotide-free

Structural highlights

1oe9 is a 2 chain structure with sequence from Chick and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYO5A_CHICK] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity).

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

The myosin superfamily of molecular motors use ATP hydrolysis and actin-activated product release to produce directed movement and force. Although this is generally thought to involve movement of a mechanical lever arm attached to a motor core, the structural details of the rearrangement in myosin that drive the lever arm motion on actin attachment are unknown. Motivated by kinetic evidence that the processive unconventional myosin, myosin V, populates a unique state in the absence of nucleotide and actin, we obtained a 2.0 A structure of a myosin V fragment. Here we reveal a conformation of myosin without bound nucleotide. The nucleotide-binding site has adopted new conformations of the nucleotide-binding elements that reduce the affinity for the nucleotide. The major cleft in the molecule has closed, and the lever arm has assumed a position consistent with that in an actomyosin rigor complex. These changes have been accomplished by relative movements of the subdomains of the molecule, and reveal elements of the structural communication between the actin-binding interface and nucleotide-binding site of myosin that underlie the mechanism of chemo-mechanical transduction.

A structural state of the myosin V motor without bound nucleotide.,Coureux PD, Wells AL, Menetrey J, Yengo CM, Morris CA, Sweeney HL, Houdusse A Nature. 2003 Sep 25;425(6956):419-23. PMID:14508494^[1]

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

References

↑ Coureux PD, Wells AL, Menetrey J, Yengo CM, Morris CA, Sweeney HL, Houdusse A. A structural state of the myosin V motor without bound nucleotide. Nature. 2003 Sep 25;425(6956):419-23. PMID:14508494 doi:10.1038/nature01927

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/1oe9"

@@ Line 3: / Line 3: @@
 <StructureSection load='1oe9' size='340' side='right'caption='[[1oe9]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1oe9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OE9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1oe9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OE9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe9 OCA], [http://pdbe.org/1oe9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oe9 RCSB], [http://www.ebi.ac.uk/pdbsum/1oe9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oe9 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oe9 OCA], [https://pdbe.org/1oe9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oe9 RCSB], [https://www.ebi.ac.uk/pdbsum/1oe9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oe9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYO5A_CHICK MYO5A_CHICK]] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity).
+[[https://www.uniprot.org/uniprot/MYO5A_CHICK MYO5A_CHICK]] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1oe9

From Proteopedia

Revision as of 07:12, 25 August 2021

Crystal structure of Myosin V motor with essential light chain-nucleotide-free

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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