A structurally conserved water molecule in Rossmann dinucleotide-binding domains.
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ABSTRACT:
SUBMITTER: Bottoms CA
PROVIDER: S-EPMC2373605 | biostudies-literature | 2002 Sep
REPOSITORIES: biostudies-literature
Publications
A structurally conserved water molecule in Rossmann dinucleotide-binding domains.
Bottoms Christopher A CA Smith Paul E PE Tanner John J JJ
Protein science : a publication of the Protein Society 20020901 9
A computational comparison of 102 high-resolution (</=1.90 A) enzyme-dinucleotide (NAD, NADP, FAD) complexes was performed to investigate the role of solvent in dinucleotide recognition by Rossmann fold domains. The typical binding site contains about 9-12 water molecules, and about 30% of the hydrogen bonds between the protein and the dinucleotide are water mediated. Detailed inspection of the structures reveals a structurally conserved water molecule bridging dinucleotides with the well-known ...[more]
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