2KS0

Solution NMR structure of the Q251Q8_DESHY(21-82) protein from Desulfitobacterium Hafniense, Northeast Structural Genomics Consortium Target DhR8C

Summary for 2KS0

• Entry DOI: 10.2210/pdb2ks0/pdb
• NMR Information: BMRB: 16656
• Descriptor: Uncharacterized protein (1 entity in total)
• Functional Keywords: yabp family, desulfitobacterium hafniense, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
• Biological source: Desulfitobacterium hafniense
• Total number of polymer chains: 2
• Total formula weight: 16004.41

Authors

Yang, Y.,Ramelot, T.A.,Cort, J.R.,Wang, H.,Ciccosanti, C.,Foote, E.L.,Jiang, M.,Janjua, H.,Acton, T.B.,Xiao, R.,Everett, J.K.,Montelione, G.T.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2009-12-23, release date: 2010-01-12, Last modification date: 2024-05-08)

Primary citation

Yang, Y.,Ramelot, T.A.,McCarrick, R.M.,Ni, S.,Feldmann, E.A.,Cort, J.R.,Wang, H.,Ciccosanti, C.,Jiang, M.,Janjua, H.,Acton, T.B.,Xiao, R.,Everett, J.K.,Montelione, G.T.,Kennedy, M.A.
Combining NMR and EPR methods for homodimer protein structure determination.
J.Am.Chem.Soc., 132:11910-11913, 2010

PubMed Abstract: There is a general need to develop more powerful and more robust methods for structural characterization of homodimers, homo-oligomers, and multiprotein complexes using solution-state NMR methods. In recent years, there has been increasing emphasis on integrating distinct and complementary methodologies for structure determination of multiprotein complexes. One approach not yet widely used is to obtain intermediate and long-range distance constraints from paramagnetic relaxation enhancements (PRE) and electron paramagnetic resonance (EPR)-based techniques such as double electron electron resonance (DEER), which, when used together, can provide supplemental distance constraints spanning to 10-70 A. In this Communication, we describe integration of PRE and DEER data with conventional solution-state nuclear magnetic resonance (NMR) methods for structure determination of Dsy0195, a homodimer (62 amino acids per monomer) from Desulfitobacterium hafniense. Our results indicate that combination of conventional NMR restraints with only one or a few DEER distance constraints and a small number of PRE constraints is sufficient for the automatic NMR-based structure determination program CYANA to build a network of interchain nuclear Overhauser effect constraints that can be used to accurately define both the homodimer interface and the global homodimer structure. The use of DEER distances as a source of supplemental constraints as described here has virtually no upper molecular weight limit, and utilization of the PRE constraints is limited only by the ability to make accurate assignments of the protein amide proton and nitrogen chemical shifts.

PubMed: 20698532
DOI: 10.1021/ja105080h

Experimental method

SOLUTION NMR