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PDBsum entry 3aa7
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protein ligands metals Protein-protein interface(s) links
Protein binding PDB id
3aa7

 

 

 

 

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Contents
Protein chains
269 a.a. *
243 a.a. *
Ligands
MES
Metals
_BA
Waters ×290
* Residue conservation analysis
PDB id:
3aa7
Name: Protein binding
Title: Crystal structure of actin capping protein
Structure: F-actin-capping protein subunit alpha-1. Chain: a. Synonym: capz 36/32, beta-actinin subunit i. Engineered: yes. F-actin-capping protein subunit beta isoforms 1 and 2. Chain: b. Synonym: capz b1 and b2, capz 36/32, beta-actinin subunit ii. Engineered: yes. Mutation: yes.
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Gene: capza1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: capzb.
Resolution:
1.90Å     R-factor:   0.211     R-free:   0.261
Authors: S.Takeda,S.Minakata,A.Narita,M.Kitazawa,T.Yamakuni,Y.Maeda,Y.Nitanai
Key ref: S.Takeda et al. (2010). Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition. Plos Biol, 8, e1000416. PubMed id: 20625546
Date:
11-Nov-09     Release date:   04-Aug-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13127  (CAZA1_CHICK) -  F-actin-capping protein subunit alpha-1 from Gallus gallus
Seq:
Struc: 		286 a.a.
269 a.a.
Protein chain
Pfam   ArchSchema ?
P14315  (CAPZB_CHICK) -  F-actin-capping protein subunit beta isoforms 1 and 2 from Gallus gallus
Seq:
Struc: 		277 a.a.
243 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Plos Biol 8:e1000416 (2010)
PubMed id: 20625546  
 
 
Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition.
S.Takeda, S.Minakata, R.Koike, I.Kawahata, A.Narita, M.Kitazawa, M.Ota, T.Yamakuni, Y.Maéda, Y.Nitanai.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20637412 T.Oda, and Y.Maéda (2010).
Multiple Conformations of F-actin.
  Structure, 18, 761-767.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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