Ribokinase - Revision history

Alexander Berchansky at 13:08, 30 June 2022

2022-06-30T13:08:29Z

←Older revision		Revision as of 13:08, 30 June 2022
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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 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. The <scene name='91/915829/Cv/6'>ATP binding site</scene> is surrounded by hydrophobic residues.	+	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==

Alexander Berchansky at 11:49, 30 June 2022

2022-06-30T11:49:53Z

←Older revision		Revision as of 11:49, 30 June 2022
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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 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. The ATP binding site is surrounded by hydrophobic residues.	+	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. The <scene name='91/915829/Cv/6'>ATP binding site</scene> is surrounded by hydrophobic residues.

	==Ribokinase 3D structures==		==Ribokinase 3D structures==

Alexander Berchansky at 13:35, 29 June 2022

2022-06-29T13:35:11Z

←Older revision		Revision as of 13:35, 29 June 2022
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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 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. The ATP binding site is surrounded by hydrophobic residues. ~~<scene name='91/915829/Cv/4'>TextToBeDisplayed</scene>~~	+	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. The ATP binding site is surrounded by hydrophobic residues.

	==Ribokinase 3D structures==		==Ribokinase 3D structures==

Alexander Berchansky at 13:34, 29 June 2022

2022-06-29T13:34:39Z

←Older revision		Revision as of 13:34, 29 June 2022
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-	<StructureSection load='6ils' size='340' side='right' caption='Ribokinase dimer complexed with ribose, ~~ADP~~ and Na+ ion (PDB id [[6ils]])' scene='91/915829/Cv/1'>	+	<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'>


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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 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. The ATP binding site is surrounded by hydrophobic residues.	+	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. The ATP binding site is surrounded by hydrophobic residues. <scene name='91/915829/Cv/4'>TextToBeDisplayed</scene>

	==Ribokinase 3D structures==		==Ribokinase 3D structures==

Alexander Berchansky at 13:24, 29 June 2022

2022-06-29T13:24:39Z

←Older revision		Revision as of 13:24, 29 June 2022
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	== Function ==		== Function ==

-	'''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 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.	+	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. The ATP binding site is surrounded by hydrophobic residues.

	==Ribokinase 3D structures==		==Ribokinase 3D structures==

Alexander Berchansky at 12:58, 29 June 2022

2022-06-29T12:58:18Z

←Older revision		Revision as of 12:58, 29 June 2022
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-	<StructureSection load='6ils' size='340' side='right' caption='Ribokinase dimer complexed with ribose, ADP and Na+ ion (PDB id [[6ils]])' scene=''>	+	<StructureSection load='6ils' size='340' side='right' caption='Ribokinase dimer complexed with ribose, ADP and Na+ ion (PDB id [[6ils]])' scene='91/915829/Cv/1'>

Michal Harel at 09:09, 28 June 2022

2022-06-28T09:09:36Z

←Older revision		Revision as of 09:09, 28 June 2022
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-	<StructureSection load='6ils' size='340' side='right' caption='~~E. coli ribokinase~~ dimer complexed with ribose, ADP and Na+ ion (PDB id [[~~1rkd~~]])' scene=''>	+	<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.
-
-	== Disease ==
-
-	== Relevance ==

	== 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 ~~interacts~~ with residues ~~Lys43 and Thr30~~	+	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]]

Michal Harel at 08:46, 28 June 2022

2022-06-28T08:46:03Z

←Older revision		Revision as of 08:46, 28 June 2022
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-		+	<StructureSection load='6ils' size='340' side='right' caption='E. coli ribokinase dimer complexed with ribose, ADP and Na+ ion (PDB id [[1rkd]])' scene=''>
-	<StructureSection load='~~1rkd~~' size='340' side='right' caption='E. coli ribokinase complexed with ribose ~~and~~ ADP ( PDB id [[1rkd]])' scene=''>	+


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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 interacts with residues Lys43 and Thr30

	==Ribokinase 3D structures==		==Ribokinase 3D structures==

Michal Harel: New page: == Function == '''Ribokinase''' (RK) catal...

2022-06-28T08:00:46Z

New page: <StructureSection load='1rkd' size='340' side='right' caption='E. coli ribokinase complexed with ribose and ADP ( PDB id 1rkd)' scene=''> == Function == '''Ribokinase''' (RK) catal...

New page

<StructureSection load='1rkd' size='340' side='right' caption='E. coli ribokinase complexed with ribose and ADP ( PDB id [[1rkd]])' scene=''>

== Function ==

'''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.

== Disease ==

== Relevance ==

== Structural highlights ==

==Ribokinase 3D structures==
[[Ribokinase 3D structures]]
</StructureSection>
== References ==
<references/>