2MCF

NMR structure of TGAM_1934

Summary for 2MCF

• Entry DOI: 10.2210/pdb2mcf/pdb
• NMR Information: BMRB: 19438
• Descriptor: TGAM_1934 (1 entity in total)
• Functional Keywords: tgam, unknown function
• Biological source: Thermococcus gammatolerans
• Total number of polymer chains: 1
• Total formula weight: 16758.33

Authors

Yang, Y.,Montet de Guillen, K.,Roumestand, C. (deposition date: 2013-08-19, release date: 2014-09-03, Last modification date: 2024-11-27)

Primary citation

Yang, Y.S.,Fernandez, B.,Lagorce, A.,Aloin, V.,De Guillen, K.M.,Boyer, J.B.,Dedieu, A.,Confalonieri, F.,Armengaud, J.,Roumestand, C.
Prioritizing targets for structural biology through the lens of proteomics: the archaeal protein TGAM_1934 from Thermococcus gammatolerans.
Proteomics, 15:114-123, 2015

PubMed Abstract: ORFans are hypothetical proteins lacking any significant sequence similarity with other proteins. Here, we highlighted by quantitative proteomics the TGAM_1934 ORFan from the hyperradioresistant Thermococcus gammatolerans archaeon as one of the most abundant hypothetical proteins. This protein has been selected as a priority target for structure determination on the basis of its abundance in three cellular conditions. Its solution structure has been determined using multidimensional heteronuclear NMR spectroscopy. TGAM_1934 displays an original fold, although sharing some similarities with the 3D structure of the bacterial ortholog of frataxin, CyaY, a protein conserved in bacteria and eukaryotes and involved in iron-sulfur cluster biogenesis. These results highlight the potential of structural proteomics in prioritizing ORFan targets for structure determination based on quantitative proteomics data. The proteomic data and structure coordinates have been deposited to the ProteomeXchange with identifier PXD000402 (http://proteomecentral.proteomexchange.org/dataset/PXD000402) and Protein Data Bank under the accession number 2mcf, respectively.

PubMed: 25359407
DOI: 10.1002/pmic.201300535

Experimental method

SOLUTION NMR