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PDBsum entry 5trc

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protein metals Protein-protein interface(s) links
Ligase PDB id
5trc

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
426 a.a.
398 a.a.
Metals
_CL ×2
PDB id:
5trc
Name: Ligase
Title: Crystal structure of phosphorylated ac3-ac5 domains of yeast acetyl- coa carboxylase
Structure: Acetyl-coa carboxylase. Chain: a, b. Synonym: acc,fatty acid synthetase 3,mRNA transport-defective protein 7. Engineered: yes
Source: Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: acc1, abp2, fas3, mtr7, ynr016c, n3175. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.90Å     R-factor:   0.226     R-free:   0.287
Authors: J.Wei,L.Tong
Key ref: J.Wei et al. (2016). A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation. Cell Discov, 2, 16044. PubMed id: 27990296 DOI: 10.1038/celldisc.2016.44
Date:
26-Oct-16     Release date:   07-Dec-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q00955  (ACAC_YEAST) -  Acetyl-CoA carboxylase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2233 a.a.
426 a.a.
Protein chain
Pfam   ArchSchema ?
Q00955  (ACAC_YEAST) -  Acetyl-CoA carboxylase from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2233 a.a.
398 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class 2: Chains A, B: E.C.6.3.4.14  - biotin carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N6-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP = N6- carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H+
N(6)-biotinyl-L-lysyl-[protein]
+ hydrogencarbonate
+ ATP
= N(6)- carboxybiotinyl-L-lysyl-[protein]
+ ADP
+ phosphate
+ H(+)
   Enzyme class 3: Chains A, B: E.C.6.4.1.2  - acetyl-CoA carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: hydrogencarbonate + acetyl-CoA + ATP = malonyl-CoA + ADP + phosphate + H+
hydrogencarbonate
+ acetyl-CoA
+ ATP
= malonyl-CoA
+ ADP
+ phosphate
+ H(+)
      Cofactor: Biotin
Biotin
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1038/celldisc.2016.44 Cell Discov 2:16044 (2016)
PubMed id: 27990296  
 
 
A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation.
J.Wei, Y.Zhang, T.Y.Yu, K.Sadre-Bazzaz, M.J.Rudolph, G.A.Amodeo, L.S.Symington, T.Walz, L.Tong.
 
  ABSTRACT  
 
No abstract given.

 

 

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