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231225s2019 xx |||||o 00| ||eng c |
| 024 |
7 |
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|a 10.1002/jcc.25798
|2 doi
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|a pubmed24n0979.xml
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|a (DE-627)NLM293731950
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|a (NLM)30747434
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Wang, Dongdong
|e verfasserin
|4 aut
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| 245 |
1 |
3 |
|a An unconventional ligand-binding mechanism of substrate-binding proteins
|b MD simulation and Markov state model analysis of BtuF
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| 264 |
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|c 2019
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 12.08.2020
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|a Date Revised 12.08.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2019 Wiley Periodicals, Inc.
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|a In conventional "Venus Flytrap" mechanism, substrate-binding proteins (SBPs) interconvert between the open and closed conformations. Upon ligand binding, SBPs form a tightly closed conformation with the ligand bound at the interface of two domains. This mechanism was later challenged by many type III SBPs, such as the vitamin B12 -binding protein BtuF, in which the apo- and holo-state proteins adopt very similar conformations. Here, we combined molecular dynamics simulation and Markov state model analysis to study the conformational dynamics of apo- and B12 -bound BtuF. The results indicate that the crystal structures represent the only stable conformation of BtuF. Meanwhile, both apo- and holo-BtuF undergo large-scale interdomain motions with little energy cost. B12 binding casts little restraints on the interdomain motions, suggesting that ligand binding affinity is enhanced by the remaining conformational entropy of holo-BtuF. These results reveal a new paradigm of ligand recognition mechanism of SBPs. © 2019 Wiley Periodicals, Inc
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4 |
|a Journal Article
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| 650 |
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4 |
|a Research Support, Non-U.S. Gov't
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| 650 |
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4 |
|a MD simulation
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| 650 |
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4 |
|a Markov state model
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| 650 |
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4 |
|a conformational dynamics
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| 650 |
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4 |
|a intrinsic disorder
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| 650 |
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4 |
|a periplasmic binding protein
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| 650 |
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|a Escherichia coli Proteins
|2 NLM
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| 650 |
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|a Ligands
|2 NLM
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| 650 |
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7 |
|a Periplasmic Binding Proteins
|2 NLM
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| 650 |
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7 |
|a btuF protein, E coli
|2 NLM
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| 700 |
1 |
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|a Weng, Jingwei
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wang, Wenning
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Journal of computational chemistry
|d 1984
|g 40(2019), 14 vom: 30. Mai, Seite 1440-1448
|w (DE-627)NLM098138448
|x 1096-987X
|7 nnns
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| 773 |
1 |
8 |
|g volume:40
|g year:2019
|g number:14
|g day:30
|g month:05
|g pages:1440-1448
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| 856 |
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|u http://dx.doi.org/10.1002/jcc.25798
|3 Volltext
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