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PDBsum entry 4z79

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protein ligands metals links
Protein binding PDB id
4z79

 

 

 

 

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Contents
Protein chain
173 a.a.
Ligands
GOL ×6
Metals
_NA ×3
_CL
Waters ×191
PDB id:
4z79
Name: Protein binding
Title: Leiomodin-1 actin-binding site 2 (abs2)
Structure: Leiomodin-1 actin-binding site 2 (abs2). Chain: a. Fragment: unp residues 299-486. Synonym: 64 kda autoantigen 1d,64 kda autoantigen 1d3,64 kda autoantigen d1,leiomodin,muscle form,smooth muscle leiomodin,sm-lmod, thyroid-associated ophthalmopathy autoantigen. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: lmod1. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.54Å     R-factor:   0.157     R-free:   0.177
Authors: G.Rebowski,M.Boczkowska,R.Dominguez
Key ref: M.Boczkowska et al. (2015). How Leiomodin and Tropomodulin use a common fold for different actin assembly functions. Nat Commun, 6, 8314. PubMed id: 26370058 DOI: 10.1038/ncomms9314
Date:
06-Apr-15     Release date:   21-Oct-15    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P29536  (LMOD1_HUMAN) -  Leiomodin-1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
600 a.a.
173 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1038/ncomms9314 Nat Commun 6:8314 (2015)
PubMed id: 26370058  
 
 
How Leiomodin and Tropomodulin use a common fold for different actin assembly functions.
M.Boczkowska, G.Rebowski, E.Kremneva, P.Lappalainen, R.Dominguez.
 
  ABSTRACT  
 
How proteins sharing a common fold have evolved different functions is a fundamental question in biology. Tropomodulins (Tmods) are prototypical actin filament pointed-end-capping proteins, whereas their homologues, Leiomodins (Lmods), are powerful filament nucleators. We show that Tmods and Lmods do not compete biochemically, and display similar but distinct localization in sarcomeres. Changes along the polypeptide chains of Tmods and Lmods exquisitely adapt their functions for capping versus nucleation. Tmods have alternating tropomyosin (TM)- and actin-binding sites (TMBS1, ABS1, TMBS2 and ABS2). Lmods additionally contain a C-terminal extension featuring an actin-binding WH2 domain. Unexpectedly, the different activities of Tmods and Lmods do not arise from the Lmod-specific extension. Instead, nucleation by Lmods depends on two major adaptations-the loss of pointed-end-capping elements present in Tmods and the specialization of the highly conserved ABS2 for recruitment of two or more actin subunits. The WH2 domain plays only an auxiliary role in nucleation.
 

 

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