117e: Difference between revisions
No edit summary |
No edit summary |
||
| Line 31: | Line 31: | ||
[[Category: mutan structures]] | [[Category: mutan structures]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Oct 28 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Oct 28 17:38:19 2007'' | ||
Revision as of 18:33, 28 October 2007
|
THE R78K AND D117E ACTIVE SITE VARIANTS OF SACCHAROMYCES CEREVISIAE SOLUBLE INORGANIC PYROPHOSPHATASE: STRUCTURAL STUDIES AND MECHANISTIC IMPLICATIONS
OverviewOverview
We have solved the structure of two active-site variants of soluble, inorganic pyrophosphatases (PPase), R78K and D117K, at resolutions of 1.85, and 2.15 A and R-factors of 19.5% and 18.3%, respectively.In the R78K, variant structure, the high-affinity phosphate group (P1) is missing, consistent with the wild-type structure showing a bidentate interaction, between P1 and Arg78, and solution data showing a decrease in P1 affinity, in the variant. The structure explains why the mutation affects P1 and, pyrophosphate binding much more than would be expected by the loss of one, hydrogen bond: Lys78 forms an ion-pair with Asp71, precluding an, interaction with P1. The R78K variant also provides the first direct, evidence that the low-affinity phosphate group (P2) can adopt the, structure that ... [(full description)]
About this StructureAbout this Structure
117E is a [Single protein] structure of sequence from [SACCHAROMYCES CEREVISIAE] with MN and PO4 as [ligands].
ReferenceReference
The R78K and D117E active-site variants of Saccharomyces cerevisiae soluble inorganic pyrophosphatase: structural studies and mechanistic implications., Tuominen V, Heikinheimo P, Kajander T, Torkkel T, Hyytia T, Kapyla J, Lahti R, Cooperman BS, Goldman A, J Mol Biol. 1998 Dec 18;284(5):1565-80. PMID:9878371
Page seeded by OCA on Sun Oct 28 17:38:19 2007