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| - | [[Image:1nhh.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1nhh| PDB=1nhh | SCENE= }} | | {{STRUCTURE_1nhh| PDB=1nhh | SCENE= }} |
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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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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12782329}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12782329 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12782329}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mutl]] | | [[Category: Mutl]] |
| | [[Category: Rubidium]] | | [[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 Sun Jul 27 19:05:14 2008'' |
Revision as of 16:05, 27 July 2008
Template:STRUCTURE 1nhh
Crystal structure of N-terminal 40KD MutL protein (LN40) complex with ADPnP and one Rubidium
Template:ABSTRACT PUBMED 12782329
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 Sun Jul 27 19:05:14 2008
