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4DM4

The conserved domain of yeast Cdc73

Summary for 4DM4
Entry DOI10.2210/pdb4dm4/pdb
DescriptorCell division control protein 73 (2 entities in total)
Functional Keywordspaf1 complex, gtpase-like, transcription elongation, protein binding, nucleus, transcription
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
Cellular locationNucleus, nucleoplasm: Q06697
Total number of polymer chains2
Total formula weight40241.80
Authors
Chen, H.,Shi, N.,Gao, Y.,Li, X.,Niu, L.,Teng, M. (deposition date: 2012-02-06, release date: 2012-08-22, Last modification date: 2024-03-20)
Primary citationChen, H.,Shi, N.,Gao, Y.,Li, X.,Teng, M.,Niu, L.
Crystallographic analysis of the conserved C-terminal domain of transcription factor Cdc73 from Saccharomyces cerevisiae reveals a GTPase-like fold.
Acta Crystallogr.,Sect.D, 68:953-959, 2012
Cited by
PubMed Abstract: The yeast Paf1 complex (Paf1C), which is composed of the proteins Paf1, Cdc73, Ctr9, Leo1 and Rtf1, accompanies RNA polymerase II from the promoter to the 3'-end formation site of mRNA- and snoRNA-encoding genes. As one of the first identified subunits of Paf1C, yeast Cdc73 (yCdc73) takes part in many transcription-related processes, including binding to RNA polymerase II, recruitment and activation of histone-modification factors and communication with other transcriptional activators. The human homologue of yCdc73, parafibromin, has been identified as a tumour suppressor linked to breast, renal and gastric cancers. However, the functional mechanism of yCdc73 has until recently been unclear. Here, a 2.2 Å resolution crystal structure of the highly conserved C-terminal region of yCdc73 is reported. It revealed that yCdc73 appears to have a GTPase-like fold. However, no GTPase activity was observed. The crystal structure of yCdc73 will shed new light on the modes of function of Cdc73 and Paf1C.
PubMed: 22868760
DOI: 10.1107/S0907444912017325
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.19 Å)
Structure validation

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