1nhi

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[[Image:1nhi.jpg|left|200px]]<br /><applet load="1nhi" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nhi.jpg|left|200px]]
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caption="1nhi, resolution 2.00&Aring;" />
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'''Crystal structure of N-terminal 40KD MutL (LN40) complex with ADPnP and one potassium'''<br />
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{{Structure
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|PDB= 1nhi |SIZE=350|CAPTION= <scene name='initialview01'>1nhi</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene>
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|ACTIVITY=
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|GENE= mutL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of N-terminal 40KD MutL (LN40) complex with ADPnP and one potassium'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NHI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHI OCA].
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1NHI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NHI OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12782329 12782329]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12782329 12782329]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: rubidium]]
[[Category: rubidium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:56:58 2008''

Revision as of 10:56, 20 March 2008

Image:1nhi.jpg


PDB ID 1nhi

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , , and
Gene: mutL (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of N-terminal 40KD MutL (LN40) complex with ADPnP and one potassium


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

1NHI 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

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