2q1n: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
m Protected "2q1n" [edit=sysop:move=sysop]
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2q1n.png|left|200px]]


<!--
==Actin Dimer Cross-linked Between Residues 41 and 374==
The line below this paragraph, containing "STRUCTURE_2q1n", creates the "Structure Box" on the page.
<StructureSection load='2q1n' size='340' side='right'caption='[[2q1n]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2q1n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q1N FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LAR:LATRUNCULIN+A'>LAR</scene></td></tr>
{{STRUCTURE_2q1n|  PDB=2q1n  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q1n OCA], [https://pdbe.org/2q1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q1n RCSB], [https://www.ebi.ac.uk/pdbsum/2q1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q1n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of actin in its monomeric form is known at high resolution, while the structure of filamentous F-actin is only understood at considerably lower resolution. Knowing precisely how the monomers of actin fit together would lead to a deeper understanding of the dynamic behavior of the actin filament. Here, a series of crystal structures of actin dimers are reported which were prepared by cross-linking in either the longitudinal or the lateral direction in the filament state. Laterally cross-linked dimers, comprised of monomers belonging to different protofilaments, are found to adopt configurations in crystals that are not related to the native structure of filamentous actin. In contrast, multiple structures of longitudinal dimers consistently reveal the same interface between monomers within a single protofilament. The reappearance of the same longitudinal interface in multiple crystal structures adds weight to arguments that the interface visualized is similar to that in actin filaments. Highly conserved atomic interactions involving residues 199-205 and 287-291 are highlighted.


===Actin Dimer Cross-linked Between Residues 41 and 374===
Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.,Sawaya MR, Kudryashov DS, Pashkov I, Adisetiyo H, Reisler E, Yeates TO Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):454-65. Epub 2008, Mar 19. PMID:18391412<ref>PMID:18391412</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_18391412}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2q1n" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 18391412 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18391412}}
 
==About this Structure==
[[2q1n]] is a 2 chain structure of [[Actin]] with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q1N OCA].


==See Also==
==See Also==
*[[Actin]]
*[[Actin 3D structures|Actin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:18391412</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Adisetiyo, H.]]
[[Category: Adisetiyo H]]
[[Category: Kudryashov, D S.]]
[[Category: Kudryashov DS]]
[[Category: Pashkov, I.]]
[[Category: Pashkov I]]
[[Category: Reisler, E.]]
[[Category: Reisler E]]
[[Category: Sawaya, M R.]]
[[Category: Sawaya MR]]
[[Category: Yeates, T O.]]
[[Category: Yeates TO]]
[[Category: Cross-linked dimer]]
[[Category: Structural protein]]

Latest revision as of 14:15, 30 August 2023

Actin Dimer Cross-linked Between Residues 41 and 374Actin Dimer Cross-linked Between Residues 41 and 374

Structural highlights

2q1n is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Publication Abstract from PubMed

The structure of actin in its monomeric form is known at high resolution, while the structure of filamentous F-actin is only understood at considerably lower resolution. Knowing precisely how the monomers of actin fit together would lead to a deeper understanding of the dynamic behavior of the actin filament. Here, a series of crystal structures of actin dimers are reported which were prepared by cross-linking in either the longitudinal or the lateral direction in the filament state. Laterally cross-linked dimers, comprised of monomers belonging to different protofilaments, are found to adopt configurations in crystals that are not related to the native structure of filamentous actin. In contrast, multiple structures of longitudinal dimers consistently reveal the same interface between monomers within a single protofilament. The reappearance of the same longitudinal interface in multiple crystal structures adds weight to arguments that the interface visualized is similar to that in actin filaments. Highly conserved atomic interactions involving residues 199-205 and 287-291 are highlighted.

Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.,Sawaya MR, Kudryashov DS, Pashkov I, Adisetiyo H, Reisler E, Yeates TO Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):454-65. Epub 2008, Mar 19. PMID:18391412[1]

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

See Also

References

  1. ↑ Sawaya MR, Kudryashov DS, Pashkov I, Adisetiyo H, Reisler E, Yeates TO. Multiple crystal structures of actin dimers and their implications for interactions in the actin filament. Acta Crystallogr D Biol Crystallogr. 2008 Apr;64(Pt 4):454-65. Epub 2008, Mar 19. PMID:18391412 doi:10.1107/S0907444908003351

2q1n, resolution 2.70Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2q1n&oldid=3854375"