1ehw

<StructureSection load='1ehw' size='340' side='right' caption='[[1ehw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ehw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EHW FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ehw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehw OCA], [http://pdbe.org/1ehw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ehw RCSB], [http://www.ebi.ac.uk/pdbsum/1ehw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ehw ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/NDKM_HUMAN NDKM_HUMAN]] Major role in the synthesis of nucleoside triphosphates other than ATP (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eh/1ehw_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10799505</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ehw" style="background-color:#fffaf0;"></div>

*[[Nucleoside diphosphate kinase|Nucleoside diphosphate kinase]]

[[Category: Nucleoside-diphosphate kinase]]

[[Category: Capeau, J]]

[[Category: Chiadmi, M]]

[[Category: Janin, J]]

[[Category: Johansson, M]]

[[Category: Karlsson, A]]

[[Category: Lacombe, M L]]

[[Category: Lascu, I]]

[[Category: Meyer, P]]

[[Category: Milon, L]]

[[Category: Munier, A]]

[[Category: Transferase]]