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| | <StructureSection load='6jig' size='340' side='right'caption='[[6jig]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='6jig' size='340' side='right'caption='[[6jig]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jig]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trybb Trybb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JIG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JIG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jig]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JIG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 1.903Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/GMP_reductase GMP reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.7 1.7.1.7] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jig OCA], [http://pdbe.org/6jig PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jig RCSB], [http://www.ebi.ac.uk/pdbsum/6jig PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jig ProSAT]</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=6jig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jig OCA], [https://pdbe.org/6jig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jig RCSB], [https://www.ebi.ac.uk/pdbsum/6jig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jig ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q57ZS7_TRYB2 Q57ZS7_TRYB2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: GMP reductase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trybb]] | + | [[Category: Trypanosoma brucei brucei]] |
| - | [[Category: Imamura, A]] | + | [[Category: Imamura A]] |
| - | [[Category: Inui, T]] | + | [[Category: Inui T]] |
| - | [[Category: Mase, H]] | + | [[Category: Mase H]] |
| - | [[Category: Nishimura, S]] | + | [[Category: Nishimura S]] |
| - | [[Category: 5'-monophosphate reductase]]
| + | |
| - | [[Category: Cystathionine beta synthase motif]]
| + | |
| - | [[Category: Guanosine 5'-monophosphate]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Trypanosoma brucei]]
| + | |
| Structural highlights
Function
Q57ZS7_TRYB2
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. Allosteric regulation accompanied by oligomeric state changes of Trypanosoma brucei GMP reductase through cystathionine-beta-synthase domain. Nat Commun. 2020 Apr 15;11(1):1837. doi: 10.1038/s41467-020-15611-3. PMID:32296055 doi:http://dx.doi.org/10.1038/s41467-020-15611-3
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