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PDBsum entry 4x8h
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References listed in PDB file
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Key reference
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Title
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Structural basis for catalytically restrictive dynamics of a high-Energy enzyme state.
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Authors
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M.Kovermann,
J.Ådén,
C.Grundström,
A.E.Sauer-Eriksson,
U.H.Sauer,
M.Wolf-Watz.
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Ref.
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Nat Commun, 2015,
6,
7644.
[DOI no: ]
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PubMed id
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Abstract
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An emerging paradigm in enzymology is that transient high-energy structural
states play crucial roles in enzymatic reaction cycles. Generally, these
high-energy or 'invisible' states cannot be studied directly at atomic
resolution using existing structural and spectroscopic techniques owing to their
low populations or short residence times. Here we report the direct NMR-based
detection of the molecular topology and conformational dynamics of a
catalytically indispensable high-energy state of an adenylate kinase variant. On
the basis of matching energy barriers for conformational dynamics and catalytic
turnover, it was found that the enzyme's catalytic activity is governed by its
dynamic interconversion between the high-energy state and a ground state
structure that was determined by X-ray crystallography. Our results show that it
is possible to rationally tune enzymes' conformational dynamics and hence their
catalytic power-a key aspect in rational design of enzymes catalysing novel
reactions.
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