3a5m

From Proteopedia

(Difference between revisions)

Revision as of 12:17, 29 July 2020

Crystal Structure of a Dictyostelium P109I Mg2+-Actin in Complex with Human Gelsolin Segment 1

Structural highlights

3a5m is a 2 chain structure with sequence from Atcc 11735 and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	1c0f, 3a5l, 3a5n, 3a5o
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[GELS_HUMAN] Defects in GSN are the cause of amyloidosis type 5 (AMYL5) [MIM:105120]; also known as familial amyloidosis Finnish type. AMYL5 is a hereditary generalized amyloidosis due to gelsolin amyloid deposition. It is typically characterized by cranial neuropathy and lattice corneal dystrophy. Most patients have modest involvement of internal organs, but severe systemic disease can develop in some individuals causing peripheral polyneuropathy, amyloid cardiomyopathy, and nephrotic syndrome leading to renal failure.^[1] ^[2] ^[3] ^[4]

Function

[GELS_HUMAN] Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Plays a role in ciliogenesis.^[5]

Publication Abstract from PubMed

Assembled actin filaments support cellular signaling, intracellular trafficking, and cytokinesis. ATP hydrolysis triggered by actin assembly provides the structural cues for filament turnover in vivo. Here, we present the cryo-electron microscopic (cryo-EM) structure of filamentous actin (F-actin) in the presence of phosphate, with the visualization of some alpha-helical backbones and large side chains. A complete atomic model based on the EM map identified intermolecular interactions mediated by bound magnesium and phosphate ions. Comparison of the F-actin model with G-actin monomer crystal structures reveals a critical role for bending of the conserved proline-rich loop in triggering phosphate release following ATP hydrolysis. Crystal structures of G-actin show that mutations in this loop trap the catalytic site in two intermediate states of the ATPase cycle. The combined structural information allows us to propose a detailed molecular mechanism for the biochemical events, including actin polymerization and ATPase activation, critical for actin filament dynamics.

Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release.,Murakami K, Yasunaga T, Noguchi TQ, Gomibuchi Y, Ngo KX, Uyeda TQ, Wakabayashi T Cell. 2010 Oct 15;143(2):275-87. PMID:20946985^[6]

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

References

↑ Haltia M, Prelli F, Ghiso J, Kiuru S, Somer H, Palo J, Frangione B. Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein. Biochem Biophys Res Commun. 1990 Mar 30;167(3):927-32. PMID:2157434
↑ Maury CP, Alli K, Baumann M. Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline. FEBS Lett. 1990 Jan 15;260(1):85-7. PMID:2153578
↑ Ghiso J, Haltia M, Prelli F, Novello J, Frangione B. Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type. Biochem J. 1990 Dec 15;272(3):827-30. PMID:2176481
↑ de la Chapelle A, Tolvanen R, Boysen G, Santavy J, Bleeker-Wagemakers L, Maury CP, Kere J. Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187. Nat Genet. 1992 Oct;2(2):157-60. PMID:1338910 doi:http://dx.doi.org/10.1038/ng1092-157
↑ Kim J, Lee JE, Heynen-Genel S, Suyama E, Ono K, Lee K, Ideker T, Aza-Blanc P, Gleeson JG. Functional genomic screen for modulators of ciliogenesis and cilium length. Nature. 2010 Apr 15;464(7291):1048-51. doi: 10.1038/nature08895. PMID:20393563 doi:10.1038/nature08895
↑ Murakami K, Yasunaga T, Noguchi TQ, Gomibuchi Y, Ngo KX, Uyeda TQ, Wakabayashi T. Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release. Cell. 2010 Oct 15;143(2):275-87. PMID:20946985 doi:10.1016/j.cell.2010.09.034

1 Structural highlights
2 Disease
3 Function
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/3a5m"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of a Dictyostelium P109I Mg2+-Actin in Complex with Human Gelsolin Segment 1==
-<StructureSection load='3a5m' size='340' side='right' caption='[[3a5m]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='3a5m' size='340' side='right'caption='[[3a5m]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3a5m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A5M FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3a5m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A5M FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c0f|1c0f]], [[3a5l|3a5l]], [[3a5n|3a5n]], [[3a5o|3a5o]]</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=3a5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5m OCA], [http://pdbe.org/3a5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a5m RCSB], [http://www.ebi.ac.uk/pdbsum/3a5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5m ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3a5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5m OCA], [http://pdbe.org/3a5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a5m RCSB], [http://www.ebi.ac.uk/pdbsum/3a5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5m ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 24: / Line 24: @@
 ==See Also==
-*[[Actin|Actin]]
+*[[Actin 3D structures|Actin 3D structures]]
-*[[Gelsolin|Gelsolin]]
+*[[3D Structures of gelsolin|3D Structures of gelsolin]]
 == References ==
 <references/>
@@ Line 32: / Line 32: @@
 [[Category: Atcc 11735]]
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Murakami, K]]
 [[Category: Noguchi, T Q]]

3a5m

From Proteopedia

Revision as of 12:17, 29 July 2020

Crystal Structure of a Dictyostelium P109I Mg2+-Actin in Complex with Human Gelsolin Segment 1

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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