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<StructureSection load='6lk4' size='340' side='right'caption='[[6lk4]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='6lk4' size='340' side='right'caption='[[6lk4]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6lk4]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5x8o 5x8o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LK4 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6lk4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5x8o 5x8o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LK4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.503Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6lk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lk4 OCA], [https://pdbe.org/6lk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lk4 RCSB], [https://www.ebi.ac.uk/pdbsum/6lk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lk4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q57ZS7_TRYB2 Q57ZS7_TRYB2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Guanosine 5'-monophosphate reductase (GMPR) is involved in the purine salvage pathway and is conserved throughout evolution. Nonetheless, the GMPR of Trypanosoma brucei (TbGMPR) includes a unique structure known as the cystathionine-beta-synthase (CBS) domain, though the role of this domain is not fully understood. Here, we show that guanine and adenine nucleotides exert positive and negative effects, respectively, on TbGMPR activity by binding allosterically to the CBS domain. The present structural analyses revealed that TbGMPR forms an octamer that shows a transition between relaxed and twisted conformations in the absence and presence of guanine nucleotides, respectively, whereas the TbGMPR octamer dissociates into two tetramers when ATP is available instead of guanine nucleotides. These findings demonstrate that the CBS domain plays a key role in the allosteric regulation of TbGMPR by facilitating the transition of its oligomeric state depending on ligand nucleotide availability. | |||
Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-beta-synthase domain.,Imamura A, Okada T, Mase H, Otani T, Kobayashi T, Tamura M, Kubata BK, Inoue K, Rambo RP, Uchiyama S, Ishii K, Nishimura S, Inui T Nat Commun. 2020 Apr 15;11(1):1837. doi: 10.1038/s41467-020-15611-3. PMID:32296055<ref>PMID:32296055</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6lk4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Imamura | [[Category: Trypanosoma brucei brucei]] | ||
[[Category: Inui | [[Category: Imamura A]] | ||
[[Category: Mase | [[Category: Inui T]] | ||
[[Category: Nishimura | [[Category: Mase H]] | ||
[[Category: Otani | [[Category: Nishimura S]] | ||
[[Category: Otani T]] | |||
Latest revision as of 14:02, 22 November 2023
Crystal structure of GMP reductase from Trypanosoma brucei in complex with guanosine 5'-triphosphateCrystal structure of GMP reductase from Trypanosoma brucei in complex with guanosine 5'-triphosphate
Structural highlights
FunctionPublication Abstract from PubMedGuanosine 5'-monophosphate reductase (GMPR) is involved in the purine salvage pathway and is conserved throughout evolution. Nonetheless, the GMPR of Trypanosoma brucei (TbGMPR) includes a unique structure known as the cystathionine-beta-synthase (CBS) domain, though the role of this domain is not fully understood. Here, we show that guanine and adenine nucleotides exert positive and negative effects, respectively, on TbGMPR activity by binding allosterically to the CBS domain. The present structural analyses revealed that TbGMPR forms an octamer that shows a transition between relaxed and twisted conformations in the absence and presence of guanine nucleotides, respectively, whereas the TbGMPR octamer dissociates into two tetramers when ATP is available instead of guanine nucleotides. These findings demonstrate that the CBS domain plays a key role in the allosteric regulation of TbGMPR by facilitating the transition of its oligomeric state depending on ligand nucleotide availability. Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-beta-synthase domain.,Imamura A, Okada T, Mase H, Otani T, Kobayashi T, Tamura M, Kubata BK, Inoue K, Rambo RP, Uchiyama S, Ishii K, Nishimura S, Inui T Nat Commun. 2020 Apr 15;11(1):1837. doi: 10.1038/s41467-020-15611-3. PMID:32296055[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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