3MCE: Crystal structure of the NAC domain of alpha subunit of nascent polypeptide-associated complex(NAC)

Citation:
Abstract
Nascent polypeptide associated complex (NAC) and its two isolated subunits, alphaNAC and betaNAC, play important roles in nascent peptide targeting. We determined a 1.9 A resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 A resolution crystal structure of alphaNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and alphaNAC homodimerization. We found that the NAC domains of alphaNAC and betaNAC 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 betaNAC 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.
PDB ID: 3MCEDownload
MMDB ID: 83339
PDB Deposition Date: 2010/3/29
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.396  Å
Source Organism:
Similar Structures:
Biological Unit for 3MCE: dimeric; determined by author and by software (PISA)
Molecular Components in 3MCE
Label Count Molecule
Proteins (2 molecules)
2
Nascent Polypeptide-associated Complex Subunit Alpha(Gene symbol: NACA)
Molecule annotation
Chemicals (5 molecules)
1
5
* Click molecule labels to explore molecular sequence information.

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