1nhh
From Proteopedia
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'''Crystal structure of N-terminal 40KD MutL protein (LN40) complex with ADPnP and one Rubidium''' | '''Crystal structure of N-terminal 40KD MutL protein (LN40) complex with ADPnP and one Rubidium''' | ||
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[[Category: Machius, M.]] | [[Category: Machius, M.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
| - | [[Category: | + | [[Category: Atpase]] |
| - | [[Category: | + | [[Category: Dna mismatch repair]] |
| - | [[Category: | + | [[Category: Mutl]] |
| - | [[Category: | + | [[Category: Rubidium]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:32:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:32, 2 May 2008
Crystal structure of N-terminal 40KD MutL protein (LN40) complex with ADPnP and one Rubidium
Overview
The GHKL phosphotransferase superfamily, characterized by four sequence motifs that form the ATP-binding site, consists of the ATPase domains of type II DNA topoisomerases, Hsp90, and MutL, and bacterial and mitochondrial protein kinases. In addition to a magnesium ion, which is essential for catalysis, a potassium ion bound adjacent to the triphosphate moiety of ATP in a rat mitochondrial protein kinase, BCK (branched-chain alpha-ketoacid dehydrogenase kinase), has been shown to be indispensable for nucleotide binding and hydrolysis. Using X-ray crystallographic, biochemical, and genetic analyses, we find that the monovalent cation-binding site is conserved in MutL, but both Na(+) and K(+) support the MutL ATPase activity. When Ala100 of MutL is substituted by proline, mimicking the K(+)-binding environment in BCK, the mutant MutL protein becomes exclusively dependent on Na(+) for the ATPase activity. The coordination of this Na(+) ion is identical to that of the K(+) ion in BCK and involves four carbonyl oxygen atoms emanating from the hinges of the ATP lid and a non-bridging oxygen of the bound nucleotide. A similar monovalent cation-binding site is found in DNA gyrase with additional coordination by a serine side chain. The conserved and protein-specific monovalent cation-binding site is unique to the GHKL superfamily and probably essential for both ATPase and kinase activity. Dependence on different monovalent cations for catalysis may be exploited for future drug design specifically targeting each individual member of the GHKL superfamily.
About this Structure
1NHH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Monovalent cation dependence and preference of GHKL ATPases and kinases., Hu X, Machius M, Yang W, FEBS Lett. 2003 Jun 5;544(1-3):268-73. PMID:12782329 Page seeded by OCA on Sat May 3 02:32:08 2008
Categories: Escherichia coli | Single protein | Hu, X. | Machius, M. | Yang, W. | Atpase | Dna mismatch repair | Mutl | Rubidium
