Ribokinase: Difference between revisions
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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, ADP and Na+ ion (PDB id [[6ils]])' scene=''> | ||
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'''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. | '''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. | ||
== 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>. The binding site is lined with charged residues. The ATP binding site is surrounded by hydrophobic residues. | ||
==Ribokinase 3D structures== | ==Ribokinase 3D structures== | ||
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== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | |||
