1RTY

Crystal Structure of Bacillus subtilis YvqK, a putative ATP-binding Cobalamin Adenosyltransferase, The North East Structural Genomics Target SR128

Summary for 1RTY

• Entry DOI: 10.2210/pdb1rty/pdb
• Descriptor: yvqk protein, PHOSPHATE ION (3 entities in total)
• Functional Keywords: all alpha-helical trimeric protein, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Potential): O34899
• Total number of polymer chains: 3
• Total formula weight: 64934.16

Authors

Forouhar, F.,Lee, I.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Tong, L.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2003-12-10, release date: 2003-12-23, Last modification date: 2024-11-20)

Primary citation

Forouhar, F.,Kuzin, A.,Seetharaman, J.,Lee, I.,Zhou, W.,Abashidze, M.,Chen, Y.,Yong, W.,Janjua, H.,Fang, Y.,Wang, D.,Cunningham, K.,Xiao, R.,Acton, T.B.,Pichersky, E.,Klessig, D.F.,Porter, C.W.,Montelione, G.T.,Tong, L.
Functional insights from structural genomics.
J.STRUCT.FUNCT.GENOM., 8:37-44, 2007

PubMed Abstract: Structural genomics efforts have produced structural information, either directly or by modeling, for thousands of proteins over the past few years. While many of these proteins have known functions, a large percentage of them have not been characterized at the functional level. The structural information has provided valuable functional insights on some of these proteins, through careful structural analyses, serendipity, and structure-guided functional screening. Some of the success stories based on structures solved at the Northeast Structural Genomics Consortium (NESG) are reported here. These include a novel methyl salicylate esterase with important role in plant innate immunity, a novel RNA methyltransferase (H. influenzae yggJ (HI0303)), a novel spermidine/spermine N-acetyltransferase (B. subtilis PaiA), a novel methyltransferase or AdoMet binding protein (A. fulgidus AF_0241), an ATP:cob(I)alamin adenosyltransferase (B. subtilis YvqK), a novel carboxysome pore (E. coli EutN), a proline racemase homolog with a disrupted active site (B. melitensis BME11586), an FMN-dependent enzyme (S. pneumoniae SP_1951), and a 12-stranded beta-barrel with a novel fold (V. parahaemolyticus VPA1032).

PubMed: 17588214
DOI: 10.1007/s10969-007-9018-3

Experimental method

X-RAY DIFFRACTION (2.4 Å)