Ribokinase
From Proteopedia
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| - | <StructureSection load='6ils' size='340' side='right' caption=' | + | <StructureSection load='6ils' size='340' side='right' caption='Ribokinase dimer complexed with ribose, ATP and Na+ ion (PDB id [[6ils]])' scene='91/915829/Cv/1'> |
== Function == | == Function == | ||
| - | '''Ribokinase''' (RK) catalyzes the first step of ribose metabolism by phosphorylating it at the O5' position <ref>PMID:10438599</ref>. | + | '''Ribokinase''' (RK) catalyzes the first step of ribose metabolism by phosphorylating it at the O5' position <ref>PMID:10438599</ref>. ATP serves as the co-substrate of RK. |
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== Structural highlights == | == Structural highlights == | ||
| - | Upon forming a ternary complex of RK, ribose and nucleotide the RK dimer changes its open form to a closed one. The ribose substrate | + | Upon forming a ternary complex of RK, ribose and nucleotide the RK dimer changes its open form to a closed one. The ribose substrate is seen between a small β-sheel domain and the concave side of the central β sheet<ref>PMID:30822455</ref>. <scene name='91/915829/Cv/3'>The ribose binding site</scene> is lined with charged residues. Water molecules are shown as red spheres. The <scene name='91/915829/Cv/6'>ATP binding site</scene> is surrounded by hydrophobic residues. <scene name='91/915829/Cv/7'>Na coordination site</scene>. |
==Ribokinase 3D structures== | ==Ribokinase 3D structures== | ||
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== References == | == References == | ||
<references/> | <references/> | ||
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Current revision
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References
- ↑ Sigrell JA, Cameron AD, Mowbray SL. Induced fit on sugar binding activates ribokinase. J Mol Biol. 1999 Jul 30;290(5):1009-18. PMID:10438599 doi:10.1006/jmbi.1999.2938
- ↑ Kang PA, Oh J, Lee H, Witte CP, Rhee S. Crystal structure and mutational analyses of ribokinase from Arabidopsis thaliana. J Struct Biol. 2019 Feb 26. pii: S1047-8477(19)30030-9. doi:, 10.1016/j.jsb.2019.02.007. PMID:30822455 doi:http://dx.doi.org/10.1016/j.jsb.2019.02.007
