1ndp

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|PDB= 1ndp |SIZE=350|CAPTION= <scene name='initialview01'>1ndp</scene>, resolution 2.2&Aring;
|PDB= 1ndp |SIZE=350|CAPTION= <scene name='initialview01'>1ndp</scene>, resolution 2.2&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|ACTIVITY= [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]
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|ACTIVITY= <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>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ndp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndp OCA], [http://www.ebi.ac.uk/pdbsum/1ndp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ndp RCSB]</span>
}}
}}
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[[Category: Morera, S.]]
[[Category: Morera, S.]]
[[Category: Veron, M.]]
[[Category: Veron, M.]]
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[[Category: ADP]]
 
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[[Category: MG]]
 
[[Category: phosphotransferase]]
[[Category: phosphotransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:53:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:57 2008''

Revision as of 19:28, 30 March 2008


PDB ID 1ndp

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: ,
Activity: Nucleoside-diphosphate kinase, with EC number 2.7.4.6
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ADENOSINE 5'-DIPHOSPHATE BINDING AND THE ACTIVE SITE OF NUCLEOSIDE DIPHOSPHATE KINASE


Overview

The X-ray structure of nucleoside diphosphate kinase (NDP kinase) from the slime mold Dictyostelium discoideum has been determined to 2.2-A resolution and refined to an R-factor of 0.19 with and without bound ADP-Mg2+. The nucleotide binds near His 122, a residue which becomes phosphorylated during the catalytic cycle. The mode of binding is different from that observed in other phosphokinases, and it involves no glycine-rich sequence. The adenine base makes only nonpolar contacts with the protein. It points outside, explaining the lack of specificity of NDP kinase toward the base. The ribose 2'- and 3'-hydroxyls and the pyrophosphate moiety are H-bonded to polar side chains. A Mg2+ ion bridges the alpha- to the beta-phosphate which approaches the imidazole group of His 122 from the N delta side. The geometry at the active site in the ADP-Mg2+ complex suggests a mechanism for catalysis whereby the gamma-phosphate of a nucleoside triphosphate can be transferred onto His 122 with a minimum of atomic motion.

About this Structure

1NDP is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

Adenosine 5'-diphosphate binding and the active site of nucleoside diphosphate kinase., Morera S, Lascu I, Dumas C, LeBras G, Briozzo P, Veron M, Janin J, Biochemistry. 1994 Jan 18;33(2):459-67. PMID:8286376

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