5im3: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "5im3" [edit=sysop:move=sysop]
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Crystal structure of the class I ribonucleotide reductase from Pseudomonas aeruginosa in complex with dATP==
==Crystal structure of the class I ribonucleotide reductase from Pseudomonas aeruginosa in complex with dATP==
<StructureSection load='5im3' size='340' side='right' caption='[[5im3]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5im3' size='340' side='right'caption='[[5im3]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5im3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IM3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5im3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IM3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.298&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonucleoside-diphosphate_reductase Ribonucleoside-diphosphate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.4.1 1.17.4.1] </span></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5im3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5im3 OCA], [http://pdbe.org/5im3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5im3 RCSB], [http://www.ebi.ac.uk/pdbsum/5im3 PDBsum]</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=5im3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5im3 OCA], [https://pdbe.org/5im3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5im3 RCSB], [https://www.ebi.ac.uk/pdbsum/5im3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5im3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q9I4I1_PSEAE Q9I4I1_PSEAE]] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.[RuleBase:RU003410]  
[https://www.uniprot.org/uniprot/Q9I4I1_PSEAE Q9I4I1_PSEAE] Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.[RuleBase:RU003410]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 19: Line 19:
</div>
</div>
<div class="pdbe-citations 5im3" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5im3" style="background-color:#fffaf0;"></div>
==See Also==
*[[Ribonucleotide reductase 3D structures|Ribonucleotide reductase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ribonucleoside-diphosphate reductase]]
[[Category: Large Structures]]
[[Category: Johansson, R]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Logan, D T]]
[[Category: Johansson R]]
[[Category: Allosteric regulation]]
[[Category: Logan DT]]
[[Category: Atp cone]]
[[Category: Oxidoreductase]]
[[Category: Ten-stranded alpha-beta barrel]]

Latest revision as of 17:01, 30 August 2023

Crystal structure of the class I ribonucleotide reductase from Pseudomonas aeruginosa in complex with dATPCrystal structure of the class I ribonucleotide reductase from Pseudomonas aeruginosa in complex with dATP

Structural highlights

5im3 is a 2 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.298Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9I4I1_PSEAE Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.[RuleBase:RU003410]

Publication Abstract from PubMed

Ribonucleotide reductases (RNRs) reduce ribonucleotides to deoxyribonucleotides. Their overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures. The crystal structure and solution X-ray scattering data of a novel dATP-induced homotetramer of the Pseudomonas aeruginosa class I RNR reveal the structural bases for its unique properties, namely one ATP cone that binds two dATP molecules and a second one that is non-functional, binding no nucleotides. Mutations in the observed tetramer interface ablate oligomerization and dATP-induced inhibition but not the ability to bind dATP. Sequence analysis shows that the novel type of ATP cone may be widespread in RNRs. The present study supports a scenario in which diverse mechanisms for allosteric activity regulation are gained and lost through acquisition and evolutionary erosion of different types of ATP cone.

Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones.,Johansson R, Jonna VR, Kumar R, Nayeri N, Lundin D, Sjoberg BM, Hofer A, Logan DT Structure. 2016 Apr 27. pii: S0969-2126(16)30036-3. doi:, 10.1016/j.str.2016.03.025. PMID:27133024[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Johansson R, Jonna VR, Kumar R, Nayeri N, Lundin D, Sjoberg BM, Hofer A, Logan DT. Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones. Structure. 2016 Apr 27. pii: S0969-2126(16)30036-3. doi:, 10.1016/j.str.2016.03.025. PMID:27133024 doi:http://dx.doi.org/10.1016/j.str.2016.03.025

5im3, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA