3MCE

Crystal structure of the NAC domain of alpha subunit of nascent polypeptide-associated complex(NAC)

Summary for 3MCE

• Entry DOI: 10.2210/pdb3mce/pdb
• Related: 3MCB
• Descriptor: Nascent polypeptide-associated complex subunit alpha, IODIDE ION (3 entities in total)
• Functional Keywords: beta-barrel like structure, nac, homodimer, chaperone
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q13765
• Total number of polymer chains: 4
• Total formula weight: 27838.15

Authors

Wang, L.F.,Zhang, W.C.,Wang, L.,Zhang, X.J.C.,Li, X.M.,Rao, Z. (deposition date: 2010-03-29, release date: 2010-07-14, Last modification date: 2024-03-20)

Primary citation

Wang, L.F.,Zhang, W.C.,Wang, L.,Zhang, X.J.C.,Li, X.M.,Rao, Z.
Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit
Protein Cell, 1:406-416, 2010

PubMed Abstract: Nascent polypeptide associated complex (NAC) and its two isolated subunits, αNAC and βNAC, play important roles in nascent peptide targeting. We determined a 1.9 Å resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 Å resolution crystal structure of αNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and αNAC homodimerization. We found that the NAC domains of αNAC and βNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a βNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structure-function relationship of NAC.

PubMed: 21203952
DOI: 10.1007/s13238-010-0049-3

Experimental method

X-RAY DIFFRACTION (2.396 Å)