6JCN
Yeast dehydrodolichyl diphosphate synthase complex subunit NUS1
Summary for 6JCN
| Entry DOI | 10.2210/pdb6jcn/pdb |
| Descriptor | Dehydrodolichyl diphosphate synthase complex subunit NUS1, SULFATE ION (3 entities in total) |
| Functional Keywords | dehydrodolichyl diphosphate synthesis, rossmann-like fold, butterfly, heterodimer, yeast rer2, human ngbr, cis-prenyl transferase, transferase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 51915.11 |
| Authors | Ko, T.-P.,Ma, J.,Liu, W.,Chen, C.-C.,Guo, R.-T. (deposition date: 2019-01-29, release date: 2019-06-19, Last modification date: 2023-11-22) |
| Primary citation | Ma, J.,Ko, T.P.,Yu, X.,Zhang, L.,Ma, L.,Zhai, C.,Guo, R.T.,Liu, W.,Li, H.,Chen, C.C. Structural insights to heterodimeric cis-prenyltransferases through yeast dehydrodolichyl diphosphate synthase subunit Nus1. Biochem.Biophys.Res.Commun., 515:621-626, 2019 Cited by PubMed Abstract: The polyprenoid glycan carriers are produced by cis-prenyltransferases (cis-PTs), which function as heterodimers in metazoa and fungi or homodimers in bacteria, but both are found in plants, protista and archaea. Heterodimeric cis-PTs comprise catalytic and non-catalytic subunits while homodimeric enzymes contain two catalytic subunits. The non-catalytic subunits of cis-PT shows low sequence similarity to known cis-PTs and their structure information is of great interests. Here we report the crystal structure of Nus1, the non-catalytic subunit of cis-PT from Saccharomyces cerevisiae. We also investigate the heterodimer formation and active site conformation by constructing a homology model of Nus1 and its catalytic subunit. Nus1 does not contain an active site, but its C-terminus may participate in catalysis by interacting with the substrates bound to the catalytic subunit. These results provide important basis for further investigation of heterodimeric cis-PTs. PubMed: 31178134DOI: 10.1016/j.bbrc.2019.05.135 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.998 Å) |
Structure validation
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