7b9q: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==The SERp optimized structure of Ribonucleotide reductase from Rhodobacter sphaeroides== | ==The SERp optimized structure of Ribonucleotide reductase from Rhodobacter sphaeroides== | ||
<StructureSection load='7b9q' size='340' side='right'caption='[[7b9q]]' scene=''> | <StructureSection load='7b9q' size='340' side='right'caption='[[7b9q]], [[Resolution|resolution]] 2.78Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B9Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[7b9q]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B9Q FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7b9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b9q OCA], [https://pdbe.org/7b9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b9q RCSB], [https://www.ebi.ac.uk/pdbsum/7b9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b9q ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7b9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b9q OCA], [https://pdbe.org/7b9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b9q RCSB], [https://www.ebi.ac.uk/pdbsum/7b9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b9q ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to the corresponding deoxyribonucleotides. The catalytic activity of most RNRs depends on the formation of a dimer of the catalytic subunits. The active site is located at the interface, and part of the substrate binding site and regulatory mechanisms work across the subunit in the dimer. In this study, we describe and characterize a novel domain responsible for forming the catalytic dimer in several class II RNRs. The 3D structure of the class II RNR from Rhodobacter sphaeroides reveals a so far undescribed alpha-helical domain in the dimer interface, which is embracing the other subunit. Genetic removal of this HUG domain leads to a severe reduction of activity paired with reduced dimerization capability. In comparison with other described RNRs, the enzyme with this domain is less dependent on the presence of nucleotides to act as allosteric effectors in the formation of dimers. The HUG domain appears to serve as an interlock to keep the dimer intact and functional even at low enzyme and/or effector concentrations. | |||
HUG Domain Is Responsible for Active Dimer Stabilization in an NrdJd Ribonucleotide Reductase.,Fietze T, Wilk P, Kabinger F, Anoosheh S, Hofer A, Lundin D, Feiler CG, Weiss MS, Loderer C Biochemistry. 2022 Aug 2;61(15):1633-1641. doi: 10.1021/acs.biochem.2c00173. Epub, 2022 Jul 20. PMID:35856337<ref>PMID:35856337</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7b9q" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Feiler C]] | [[Category: Ribonucleoside-diphosphate reductase]] | ||
[[Category: Kabinger F]] | [[Category: Feiler, C]] | ||
[[Category: Loderer C]] | [[Category: Kabinger, F]] | ||
[[Category: Wilk P]] | [[Category: Loderer, C]] | ||
[[Category: Wilk, P]] | |||
[[Category: Allosteric effector]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Ribonucleotide reductase]] | |||
[[Category: Thiyl radical enzyme]] | |||
Revision as of 07:57, 3 August 2022
The SERp optimized structure of Ribonucleotide reductase from Rhodobacter sphaeroidesThe SERp optimized structure of Ribonucleotide reductase from Rhodobacter sphaeroides
Structural highlights
Publication Abstract from PubMedRibonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to the corresponding deoxyribonucleotides. The catalytic activity of most RNRs depends on the formation of a dimer of the catalytic subunits. The active site is located at the interface, and part of the substrate binding site and regulatory mechanisms work across the subunit in the dimer. In this study, we describe and characterize a novel domain responsible for forming the catalytic dimer in several class II RNRs. The 3D structure of the class II RNR from Rhodobacter sphaeroides reveals a so far undescribed alpha-helical domain in the dimer interface, which is embracing the other subunit. Genetic removal of this HUG domain leads to a severe reduction of activity paired with reduced dimerization capability. In comparison with other described RNRs, the enzyme with this domain is less dependent on the presence of nucleotides to act as allosteric effectors in the formation of dimers. The HUG domain appears to serve as an interlock to keep the dimer intact and functional even at low enzyme and/or effector concentrations. HUG Domain Is Responsible for Active Dimer Stabilization in an NrdJd Ribonucleotide Reductase.,Fietze T, Wilk P, Kabinger F, Anoosheh S, Hofer A, Lundin D, Feiler CG, Weiss MS, Loderer C Biochemistry. 2022 Aug 2;61(15):1633-1641. doi: 10.1021/acs.biochem.2c00173. Epub, 2022 Jul 20. PMID:35856337[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||