Structure of the dna binding cleft of the gene 5 protein from bacteriophage fd

作者: Alexander McPherson , Frances Jurnak , Andrew Wang , Alexander Rich , Ian Molineux

DOI: 10.1002/JSS.400100408

关键词: PolynucleotideDNA binding siteGeneDNAHMG-boxGroove (joinery)Aromatic amino acidsCrystallographyStereochemistryDNA-binding proteinBiologyGeneral Medicine

摘要: The structure of the gene 5 DNA unwinding protein from bacteriophage fd has been solved to 2.3-A resolution by X-ray diffraction techniques. molecule contains an extensive cleft region that we have identified as binding site on basis residues comprise its surface. interior groove a rather large number basic amino acid serve draw polynucleotide backbone into cleft. Arrayed along external edges are aromatic side groups in position stack upon bases and fix it place. mechanism visualize appear be fully consistent with evidence provided physical-chemical studies solution.

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