1ndp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ndp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ndp, resolution 2.2&Aring;" /> '''ADENOSINE 5'-DIPHOSPH...)
Line 1: Line 1:
-
[[Image:1ndp.jpg|left|200px]]<br /><applet load="1ndp" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ndp.jpg|left|200px]]<br /><applet load="1ndp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ndp, resolution 2.2&Aring;" />
caption="1ndp, resolution 2.2&Aring;" />
'''ADENOSINE 5'-DIPHOSPHATE BINDING AND THE ACTIVE SITE OF NUCLEOSIDE DIPHOSPHATE KINASE'''<br />
'''ADENOSINE 5'-DIPHOSPHATE BINDING AND THE ACTIVE SITE OF NUCLEOSIDE DIPHOSPHATE KINASE'''<br />
==Overview==
==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.
+
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==
==About this Structure==
-
1NDP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NDP OCA].
+
1NDP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1NDP OCA].
==Reference==
==Reference==
Line 24: Line 24:
[[Category: phosphotransferase]]
[[Category: phosphotransferase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:10:09 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:09 2008''

Revision as of 12:05, 21 February 2008


1ndp, resolution 2.2Å

Drag the structure with the mouse to rotate

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 with and as ligands. Active as Nucleoside-diphosphate kinase, with EC number 2.7.4.6 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

Page seeded by OCA on Thu Feb 21 14:05:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools