3byh: Difference between revisions

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<SX load='3byh' size='340' side='right' viewer='molstar' caption='[[3byh]], [[Resolution|resolution]] 12.00&Aring;' scene=''>
<SX load='3byh' size='340' side='right' viewer='molstar' caption='[[3byh]], [[Resolution|resolution]] 12.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3byh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BYH FirstGlance]. <br>
<table><tr><td colspan='2'>[[3byh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BYH FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PS1TP5BP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 12&#8491;</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=3byh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byh OCA], [http://pdbe.org/3byh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3byh RCSB], [http://www.ebi.ac.uk/pdbsum/3byh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3byh 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=3byh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byh OCA], [https://pdbe.org/3byh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3byh RCSB], [https://www.ebi.ac.uk/pdbsum/3byh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3byh ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ACTB_HUMAN ACTB_HUMAN] Defects in ACTB are a cause of dystonia juvenile-onset (DYTJ) [MIM:[https://omim.org/entry/607371 607371]. DYTJ is a form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYTJ patients manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss.<ref>PMID:16685646</ref>  Defects in ACTB are the cause of Baraitser-Winter syndrome type 1 (BRWS1) [MIM:[https://omim.org/entry/243310 243310]. A rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior-predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss.<ref>PMID:22366783</ref>
== Function ==
[https://www.uniprot.org/uniprot/ACTB_HUMAN ACTB_HUMAN] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3byh ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3byh ConSurf].
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many actin binding proteins have a modular architecture, and calponin-homology (CH) domains are one such structurally conserved module found in numerous proteins that interact with F-actin. The manner in which CH-domains bind F-actin has been controversial. Using cryo-EM and a single-particle approach to helical reconstruction, we have generated 12-A-resolution maps of F-actin alone and F-actin decorated with a fragment of human fimbrin (L-plastin) containing tandem CH-domains. The high resolution allows an unambiguous fit of the crystal structure of fimbrin into the map. The interaction between fimbrin ABD2 (actin binding domain 2) and F-actin is different from any interaction previously observed or proposed for tandem CH-domain proteins, showing that the structural conservation of the CH-domains does not lead to a conserved mode of interaction with F-actin. Both the stapling of adjacent actin protomers and the additional closure of the nucleotide binding cleft in F-actin when the fimbrin fragment binds may explain how fimbrin can stabilize actin filaments. A mechanism is proposed where ABD1 of fimbrin becomes activated for binding a second actin filament after ABD2 is bound to a first filament, and this can explain how mutations of residues buried in the interface between ABD2 and ABD1 can rescue temperature-sensitive defects in actin.
High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.,Galkin VE, Orlova A, Cherepanova O, Lebart MC, Egelman EH Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1494-8. Epub 2008 Jan 30. PMID:18234857<ref>PMID:18234857</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3byh" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</SX>
</SX>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cherepanova, O]]
[[Category: Cherepanova O]]
[[Category: Egelman, E H]]
[[Category: Egelman EH]]
[[Category: Galkin, V E]]
[[Category: Galkin VE]]
[[Category: Lebart, M C]]
[[Category: Lebart MC]]
[[Category: Orlova, A]]
[[Category: Orlova A]]
[[Category: Acetylation]]
[[Category: Atp-binding]]
[[Category: Cytoplasm]]
[[Category: Cytoskeleton]]
[[Category: Helical filament]]
[[Category: Methylation]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Protein polymer]]
[[Category: Structural protein]]

Latest revision as of 12:31, 21 February 2024

Model of actin-fimbrin ABD2 complexModel of actin-fimbrin ABD2 complex

3byh, resolution 12.00Å

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OCA
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