2kzm
From Proteopedia
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KLENOW FRAGMENT WITH NORMAL SUBSTRATE AND ZINC AND MANGANESE
Overview
The interaction of a divalent metal ion with a leaving 3' oxygen is a, central component of several proposed mechanisms of phosphoryl transfer., In support of this are recent kinetic studies showing that thiophilic, metal ions (e.g., Mn2+) stimulate the hydrolysis of compounds in which, sulfur takes the place of the leaving oxygen. To examine the structural, basis of this phenomenon, we have solved four crystal structures of, single-stranded DNA's containing either oxygen or sulfur at a 3'-bridging, position bound in conjunction with various metal ions at the 3'-5', exonucleolytic active site of the Klenow fragment (KF) of DNA polymerase I, from Escherichia coli. Two structures of normal ssDNA bound to KF in the, presence of Zn2+ and Mn2+ or Zn2+ alone were refined at 2.6- and 2.25-A, ... [(full description)]
About this Structure
2KZM is a [Single protein] structure of sequence from [Escherichia coli] with ZN and MN as [ligands]. Active as [DNA-directed DNA polymerase], with EC number [2.7.7.7]. Structure known Active Site: EXO. Full crystallographic information is available from [OCA].
Reference
Structures of normal single-stranded DNA and deoxyribo-3'-S-phosphorothiolates bound to the 3'-5' exonucleolytic active site of DNA polymerase I from Escherichia coli., Brautigam CA, Sun S, Piccirilli JA, Steitz TA, Biochemistry. 1999 Jan 12;38(2):696-704. PMID:9888810
Page seeded by OCA on Tue Oct 30 12:20:32 2007
