Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 105, Issue 6, Pages 1844-1848Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0711659105
Keywords
enzymatic mechanism; helium cooling; subatomic resolution crystallography; x-ray plus neutrons joint refinement
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Funding
- NCI NIH HHS [N01-CO-12400, N01CO12400] Funding Source: Medline
- NIGMS NIH HHS [R01GM071939, R01 GM071939] Funding Source: Medline
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We present results of combined studies of the enzyme human aldose reductase (h-AR, 36 kDa) using single-crystal x-ray data (0.66 angstrom, 100K; 0.80 angstrom, 15K; 1.75 angstrom, 293K), neutron Laue data (2.2 angstrom, 293K), and quantum mechanical modeling. These complementary techniques unveil the internal organization and mobility of the hydrogen bond network that defines the properties of the catalytic engine, explaining how this promiscuous enzyme overcomes the simultaneous requirements of efficiency and promiscuity offering a general mechanistic view for this class of enzymes.
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