2H25

Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin

Summary for 2H25

• Entry DOI: 10.2210/pdb2h25/pdb
• NMR Information: BMRB: 7114
• Descriptor: Maltose-binding periplasmic protein (1 entity in total)
• Functional Keywords: alpha/beta protein, sugar binding protein
• Biological source: Escherichia coli
• Cellular location: Periplasm: P0AEX9
• Total number of polymer chains: 1
• Total formula weight: 40741.10

Authors

Xu, Y.,Lin, Z.,Zheng, Y.,Yang, D. (deposition date: 2006-05-18, release date: 2006-10-31, Last modification date: 2024-05-29)

Primary citation

Xu, Y.,Zheng, Y.,Fan, J.S.,Yang, D.
A new strategy for structure determination of large proteins in solution without deuteration
Nat.Methods, 3:931-937, 2006

PubMed Abstract: So far high-resolution structure determination by nuclear magnetic resonance (NMR) spectroscopy has been limited to proteins <30 kDa, although global fold determination is possible for substantially larger proteins. Here we present a strategy for assigning backbone and side-chain resonances of large proteins without deuteration, with which one can obtain high-resolution structures from (1)H-(1)H distance restraints. The strategy uses information from through-bond correlation experiments to filter intraresidue and sequential correlations from through-space correlation experiments, and then matches the filtered correlations to obtain sequential assignment. We demonstrate this strategy on three proteins ranging from 24 to 65 kDa for resonance assignment and on maltose binding protein (42 kDa) and hemoglobin (65 kDa) for high-resolution structure determination. The strategy extends the size limit for structure determination by NMR spectroscopy to 42 kDa for monomeric proteins and to 65 kDa for differentially labeled multimeric proteins without the need for deuteration or selective labeling.

PubMed: 17060917
DOI: 10.1038/nmeth938

Experimental method

SOLUTION NMR