1ehw
From Proteopedia
(New page: 200px<br /> <applet load="1ehw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ehw, resolution 2.40Å" /> '''HUMAN NUCLEOSIDE DI...) |
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| - | [[Image:1ehw. | + | [[Image:1ehw.jpg|left|200px]]<br /><applet load="1ehw" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ehw" size=" | + | |
caption="1ehw, resolution 2.40Å" /> | caption="1ehw, resolution 2.40Å" /> | ||
'''HUMAN NUCLEOSIDE DIPHOSPHATE KINASE 4'''<br /> | '''HUMAN NUCLEOSIDE DIPHOSPHATE KINASE 4'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EHW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http:// | + | 1EHW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nucleoside diphosphate kinase]] | [[Category: nucleoside diphosphate kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:43:27 2008'' |
Revision as of 13:43, 15 February 2008
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HUMAN NUCLEOSIDE DIPHOSPHATE KINASE 4
Overview
We demonstrate here the catalytic activity and subcellular localization of, the Nm23-H4 protein, product of nm23-H4, a new member of the human, nm23/nucleoside diphosphate (NDP) kinase gene family (Milon, L., Rousseau-Merck, M., Munier, A., Erent, M., Lascu, I., Capeau, J., and, Lacombe, M. L. (1997) Hum. Genet. 99, 550-557). Nm3-H4 was synthesized in, escherichia coli as the full-length protein and as a truncated form, missing the N-terminal extension characteristic of mitochondrial, targeting. The truncated form possesses NDP kinase activity, whereas the, full-length protein is inactive, suggesting that the extension prevents, enzyme folding and/or activity. X-ray crystallographic analysis was, performed on active truncated Nm23-H4. Like other eukaryotic NDP kinases, it is a hexamer. Nm23-H4 naturally possesses a serine residue at position, 129, equivalent to the K-pn mutation of the Drosophila NDP kinase. The, x-ray structure shows that the presence of Ser(129) has local structural, effects that weaken subunit interactions. Site-directed mutagenesis shows, that the serine is responsible for the lability of Nm23-H4 to heat and, urea treatment, because the S129P mutant is greatly stabilized., Examination of human embryonic kidney 293 cells transfected with green, fluorescent protein fusions by confocal microscopy shows a specific, mitochondrial localization of Nm23-H4 that was also demonstrated by, Western blot analysis of subcellular fractions of these cells. Import into, mitochondria is accompanied by cleavage of the N-terminal extension that, results in NDP kinase activity. Submitochondrial fractionation indicates, that Nm23-H4 is associated with mitochondrial membranes, possibly to the, contact sites between the outer and inner membranes.
About this Structure
1EHW is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Nucleoside-diphosphate kinase, with EC number 2.7.4.6 Full crystallographic information is available from OCA.
Reference
The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase., Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML, J Biol Chem. 2000 May 12;275(19):14264-72. PMID:10799505
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