ISDA: 2OIG

Deposition Date 2007-01-11

Release Date 2007-03-06

Last Version Date 2024-12-25

Entry Detail

PDB ID:

2OIG

Keywords:

HYDROLASE

Title:

Crystal structure of RS21-C6 core segment and dm5CTP complex

Biological Source:

Source Organism(s):

Mus musculus (Taxon ID: 10090)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

3.30 Å

R-Value Free:

0.28

R-Value Work:

0.23

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:RS21-C6
Gene (Uniprot):Dctpp1
Chain IDs:A, B, C, D
Chain Length:111
Number of Molecules:4
Biological Source:Mus musculus

UniProt ID:Q9QY93 Pfam ID:PF12643 EC:3.6.1.12

Ligand Molecules

523

Primary Citation

Crystal Structure of RS21-C6, Involved in Nucleoside Triphosphate Pyrophosphohydrolysis

Wu, B, Liu, Y, Zhao, Q, Liao, S, Zhang, J, Bartlam, M, Chen, W, Rao, Z.Show

J. Mol. Biol. 367 1405 1412 (2007)

PMID: 17320107 DOI: 10.1016/j.jmb.2007.01.057

Abstact

RS21-C6, which is highly expressed in all vertebrate genomes and green plants, is proposed to have nucleoside triphosphate pyrophosphohydrolase activity. Here, we report the crystal structures of the core fragment of RS21-C6, named RSCUT, and the complex with the substrate 5-methyl dCTP. The refined structure of RSCUT consists mainly of alpha-helices and shows formation of a tightly associated tetramer. On the basis of the structure of the RSCUT-m5dCTP complex and the results of pyrophosphatase activity assays, several key residues involved in the substrate binding of RS21-C6 have been identified. Tetramer formation is shown to be required for substrate binding.

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Primary Citation of related structures

Abstact

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