Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

समान संसाधन

• Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit
  द्वारा: Beernink, Peter T., और अन्य
  प्रकाशित: (1999)
• Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes
  द्वारा: Endrizzi, James A., और अन्य
  प्रकाशित: (2017)
• Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains.
  द्वारा: Powers, V. M., और अन्य
  प्रकाशित: (1993)
• In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.
  द्वारा: Zhang, P., और अन्य
  प्रकाशित: (1996)
• Pathways of Assembly of Aspartate Transcarbamoylase from Catalytic and Regulatory Subunits
  द्वारा: Bothwell, M., और अन्य
  प्रकाशित: (1974)