|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution Structure of a Human Cancer-Related Nucleoside Triphosphatase== | | ==Solution Structure of a Human Cancer-Related Nucleoside Triphosphatase== |
| - | <StructureSection load='2i3b' size='340' side='right'caption='[[2i3b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2i3b' size='340' side='right'caption='[[2i3b]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2i3b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I3B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2i3b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I3B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I3B FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDRT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nucleoside-triphosphatase Nucleoside-triphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.15 3.6.1.15] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3b OCA], [https://pdbe.org/2i3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i3b RCSB], [https://www.ebi.ac.uk/pdbsum/2i3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3b ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3b OCA], [https://pdbe.org/2i3b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i3b RCSB], [https://www.ebi.ac.uk/pdbsum/2i3b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NTPCR_HUMAN NTPCR_HUMAN] Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.<ref>PMID:17291528</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nucleoside-triphosphatase]]
| + | [[Category: Almeida MS]] |
| - | [[Category: Almeida, M S]] | + | [[Category: Placzek WJ]] |
| - | [[Category: Placzek, W J]] | + | [[Category: Wuthrich K]] |
| - | [[Category: Wuthrich, K]] | + | |
| - | [[Category: Aaa]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ntpase]]
| + | |
| - | [[Category: Rossmann]]
| + | |
| Structural highlights
Function
NTPCR_HUMAN Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A screen of the human cancer genome anatomy project (CGAP) database was performed to search for new proteins involved in tumorigenesis. The resulting hits were further screened for recombinant expression, solubility and protein aggregation, which led to the identification of the previously unknown human cancer-related (HCR) protein encoded by the mRNA NM_032324 as a target for structure determination by NMR. The three-dimensional structure of the protein in its complex with ATPgammaS forms a three-layered alpha/beta sandwich, with a central nine-stranded beta-sheet surrounded by five alpha-helices. Sequence and three-dimensional structure comparisons with AAA+ ATPases revealed the presence of Walker A (GPPGVGKT) and Walker B (VCVIDEIG) motifs. Using 1D (31)P-NMR spectroscopy and a coupled enzymatic assay for the determination of inorganic phosphate, we showed that the purified recombinant protein is active as a non-specific nucleoside triphosphatase, with k(cat)=7.6x10(-3) s(-1). The structural basis for the enzymatic activity of HCR-NTPase was further characterized by site-directed mutagenesis of the Walker B motif, which further contributes to making the HCR-NTPase an attractive new target for further biochemical characterization in the context of its presumed role in human tumorigenesis.
NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase.,Placzek WJ, Almeida MS, Wuthrich K J Mol Biol. 2007 Mar 30;367(3):788-801. Epub 2007 Jan 9. PMID:17291528[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Placzek WJ, Almeida MS, Wuthrich K. NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase. J Mol Biol. 2007 Mar 30;367(3):788-801. Epub 2007 Jan 9. PMID:17291528 doi:http://dx.doi.org/10.1016/j.jmb.2007.01.001
- ↑ Placzek WJ, Almeida MS, Wuthrich K. NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase. J Mol Biol. 2007 Mar 30;367(3):788-801. Epub 2007 Jan 9. PMID:17291528 doi:http://dx.doi.org/10.1016/j.jmb.2007.01.001
|
