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PDBsum entry 5itz

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protein ligands metals Protein-protein interface(s) links
Structural protein PDB id
5itz

 

 

 

 

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Contents
Protein chains
430 a.a.
420 a.a.
13 a.a.
127 a.a.
Ligands
GTP
GDP
LOC
Metals
_MG
Waters ×473
PDB id:
5itz
Name: Structural protein
Title: Crystal structure of the sac domain of cpap in a complex with tubulin and darpin
Structure: Tubulin alpha-1b chain. Chain: a. Synonym: alpha-tubulin ubiquitous,tubulin k-alpha-1,tubulin alpha- ubiquitous chain. Tubulin beta-2b chain. Chain: b. Centromere protein j. Chain: d. Synonym: cenp-j,centrosomal p4.1-associated protein,lag-3-associated
Source: Bos taurus. Bovine. Organism_taxid: 9913. Homo sapiens. Human. Organism_taxid: 9606. Gene: cenpj, cpap, lap, lip1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.20Å     R-factor:   0.179     R-free:   0.217
Authors: A.Sharma,M.O.Steinmetz
Key ref: A.Sharma et al. (2016). Centriolar CPAP/SAS-4 Imparts Slow Processive Microtubule Growth. Dev Cell, 37, 362-376. PubMed id: 27219064 DOI: 10.1016/j.devcel.2016.04.024
Date:
17-Mar-16     Release date:   01-Jun-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P81947  (TBA1B_BOVIN) -  Tubulin alpha-1B chain from Bos taurus
Seq:
Struc:
451 a.a.
430 a.a.
Protein chain
Pfam   ArchSchema ?
Q6B856  (TBB2B_BOVIN) -  Tubulin beta-2B chain from Bos taurus
Seq:
Struc:
445 a.a.
420 a.a.*
Protein chain
Pfam   ArchSchema ?
Q9HC77  (CENPJ_HUMAN) -  Centrosomal P4.1-associated protein from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1338 a.a.
13 a.a.
Protein chain
No UniProt id for this chain
Struc: 127 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.3.6.5.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.devcel.2016.04.024 Dev Cell 37:362-376 (2016)
PubMed id: 27219064  
 
 
Centriolar CPAP/SAS-4 Imparts Slow Processive Microtubule Growth.
A.Sharma, A.Aher, N.J.Dynes, D.Frey, E.A.Katrukha, R.Jaussi, I.Grigoriev, M.Croisier, R.A.Kammerer, A.Akhmanova, P.Gönczy, M.O.Steinmetz.
 
  ABSTRACT  
 
Centrioles are fundamental and evolutionarily conserved microtubule-based organelles whose assembly is characterized by microtubule growth rates that are orders of magnitude slower than those of cytoplasmic microtubules. Several centriolar proteins can interact with tubulin or microtubules, but how they ensure the exceptionally slow growth of centriolar microtubules has remained mysterious. Here, we bring together crystallographic, biophysical, and reconstitution assays to demonstrate that the human centriolar protein CPAP (SAS-4 in worms and flies) binds and "caps" microtubule plus ends by associating with a site of β-tubulin engaged in longitudinal tubulin-tubulin interactions. Strikingly, we uncover that CPAP activity dampens microtubule growth and stabilizes microtubules by inhibiting catastrophes and promoting rescues. We further establish that the capping function of CPAP is important to limit growth of centriolar microtubules in cells. Our results suggest that CPAP acts as a molecular lid that ensures slow assembly of centriolar microtubules and, thereby, contributes to organelle length control.
 

 

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