1zip
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BACILLUS STEAROTHERMOPHILUS ADENYLATE KINASE
OverviewOverview
Crystal structures of Bacillus stearothermophilus adenylate kinase with, bound Ap5A, Mn2+ Ap5A, and Mg2+ Ap5A have been determined by X-ray, crystallography to resolutions of 1.6 A, 1.85 A, and 1.96 A, respectively., The protein's lid domain is partially open, being both rotated and, translated away from bound Ap5A. The flexibility of the lid domain in the, ternary state and its ability to transfer force directly to the the active, site is discussed in light of our proposed entropic mechanism for, catalytic turnover. The bound Zn2+ atom is demonstrably structural in, nature, with no contacts other than its ligating cysteine residues within, 5 A. The B. stearothermophilus adenylate kinase lid appears to be a, truncated zinc finger domain, lacking the DNA binding finger, which we, have ... [(full description)]
About this StructureAbout this Structure
1ZIP is a [Single protein] structure of sequence from [Geobacillus stearothermophilus] with ZN, MN and AP5 as [ligands]. Active as [[1]], with EC number [2.7.4.3]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of Bacillus stearothermophilus adenylate kinase with bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position and six coordinate octahedral geometry for bound Mg2+ and Mn2+., Berry MB, Phillips GN Jr, Proteins. 1998 Aug 15;32(3):276-88. PMID:9715904
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