Ribokinase: Difference between revisions
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<StructureSection load='6ils' size='340' side='right' caption='Ribokinase dimer complexed with ribose, | <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. | ||
== 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 is seen between a small β-sheel domain and the concave side of the central β sheet<ref>PMID:30822455</ref>. | 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== | ||
Latest revision as of 13:08, 30 June 2022
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