2h2u
From Proteopedia
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|PDB= 2h2u |SIZE=350|CAPTION= <scene name='initialview01'>2h2u</scene>, resolution 2.400Å | |PDB= 2h2u |SIZE=350|CAPTION= <scene name='initialview01'>2h2u</scene>, resolution 2.400Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Nucleoside-diphosphatase Nucleoside-diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphatase Nucleoside-diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.6 3.6.1.6] </span> |
|GENE= CANT1, SHAPY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CANT1, SHAPY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2h2n|2H2N]], [[1s18|1S18]], [[1s1d|1S1d]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2u OCA], [http://www.ebi.ac.uk/pdbsum/2h2u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h2u RCSB]</span> | ||
}} | }} | ||
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[[Category: Kirley, T L.]] | [[Category: Kirley, T L.]] | ||
[[Category: Yang, M.]] | [[Category: Yang, M.]] | ||
| - | [[Category: CA]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
[[Category: five-blade beta propeller]] | [[Category: five-blade beta propeller]] | ||
| Line 33: | Line 35: | ||
[[Category: nucleotide-binding]] | [[Category: nucleotide-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:42 2008'' |
Revision as of 00:24, 31 March 2008
| |||||||
| , resolution 2.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CANT1, SHAPY (Homo sapiens) | ||||||
| Activity: | Nucleoside-diphosphatase, with EC number 3.6.1.6 | ||||||
| Related: | 2H2N, 1S18, 1S1d
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the E130Y mutant of human soluble calcium-activated nucleotidase (SCAN) with calcium ion
Overview
Mammals express a protein homologous to soluble nucleotidases used by blood-sucking insects to inhibit host blood clotting. These vertebrate nucleotidases may play a role in protein glycosylation. The activity of this enzyme family is strictly dependent on calcium, which induces a conformational change in the secreted, soluble human nucleotidase. The crystal structure of this human enzyme was recently solved; however, the mechanism of calcium activation and the basis for the calcium-induced changes remain unclear. In this study, using analytical ultracentrifugation and chemical cross-linking, we show that calcium or strontium induce noncovalent dimerization of the soluble human enzyme. The location and nature of the dimer interface was elucidated using a combination of site-directed mutagenesis and chemical cross-linking, coupled with crystallographic analyses. Replacement of Ile(170), Ser(172), and Ser(226) with cysteine residues resulted in calcium-dependent, sulfhydryl-specific intermolecular cross-linking, which was not observed after cysteine introduction at other surface locations. Analysis of a super-active mutant, E130Y, revealed that this mutant dimerized more readily than the wild-type enzyme. The crystal structure of the E130Y mutant revealed that the mutated residue is found in the dimer interface. In addition, expression of the full-length nucleotidase revealed that this membrane-bound form can also dimerize and that these dimers are stabilized by spontaneous oxidative cross-linking of Cys(30), located between the single transmembrane helix and the start of the soluble sequence. Thus, calcium-mediated dimerization may also represent a mechanism for regulation of the activity of this nucleotidase in the physiological setting of the endoplasmic reticulum or Golgi.
About this Structure
2H2U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Calcium-dependent dimerization of human soluble calcium activated nucleotidase: characterization of the dimer interface., Yang M, Horii K, Herr AB, Kirley TL, J Biol Chem. 2006 Sep 22;281(38):28307-17. Epub 2006 Jul 11. PMID:16835225
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