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| | ==Crystal structure of GMP synthetase PH1347 from Pyrococcus horikoshii OT3== | | ==Crystal structure of GMP synthetase PH1347 from Pyrococcus horikoshii OT3== |
| - | <StructureSection load='3a4i' size='340' side='right' caption='[[3a4i]], [[Resolution|resolution]] 1.79Å' scene=''> | + | <StructureSection load='3a4i' size='340' side='right'caption='[[3a4i]], [[Resolution|resolution]] 1.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a4i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2z0c 2z0c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A4I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a4i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2z0c 2z0c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A4I FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">guaAB, PH1347 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 'Pyrococcus shinkaii'])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">guaAB, PH1347 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 'Pyrococcus shinkaii'])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/GMP_synthase_(glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.2 6.3.5.2] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/GMP_synthase_(glutamine-hydrolyzing) GMP synthase (glutamine-hydrolyzing)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.2 6.3.5.2] </span></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=3a4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a4i OCA], [http://pdbe.org/3a4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a4i RCSB], [http://www.ebi.ac.uk/pdbsum/3a4i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a4i 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=3a4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a4i OCA], [https://pdbe.org/3a4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a4i RCSB], [https://www.ebi.ac.uk/pdbsum/3a4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a4i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GUAAB_PYRHO GUAAB_PYRHO]] Catalyzes the synthesis of GMP from XMP (By similarity). | + | [[https://www.uniprot.org/uniprot/GUAAB_PYRHO GUAAB_PYRHO]] Catalyzes the synthesis of GMP from XMP (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Pyrococcus shinkaii]] | | [[Category: Pyrococcus shinkaii]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Horita, S]] | | [[Category: Horita, S]] |
| | [[Category: Lee, W C]] | | [[Category: Lee, W C]] |
| Structural highlights
Function
[GUAAB_PYRHO] Catalyzes the synthesis of GMP from XMP (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Guanosine 5'-monophosphate synthetase(s) (GMPS) catalyzes the final step of the de novo synthetic pathway of purine nucleotides. GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase (GATase) and ATP pyrophosphatase (ATPPase). GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl xanthosine 5'-monophosphate (adenyl-XMP) into guanosine 5'-monophosphate. Here we report the crystal structure of PH-ATPPase (the ATPPase subunit of the two-subunit-type GMPS from the hyperthermophilic archaeon Pyrococcus horikoshii OT3). PH-ATPPase consists of two domains (N-domain and C-domain) and exists as a homodimer in the crystal and in solution. The N-domain contains an ATP-binding platform called P-loop, whereas the C-domain contains the xanthosine 5'-monophosphate (XMP)-binding site and also contributes to homodimerization. We have also demonstrated that PH-GATase (the glutamine amidotransferase subunit of the two-subunit-type GMPS from the hyperthermophilic archaeon P. horikoshii OT3) alone is inactive, and that all substrates of PH-ATPPase except for ammonia (Mg(2+), ATP and XMP) are required to stabilize the active complex of PH-ATPPase and PH-GATase subunits.
Crystal structure of the ATPPase subunit and its substrate-dependent association with the GATase subunit: a novel regulatory mechanism for a two-subunit-type GMP synthetase from Pyrococcus horikoshii OT3.,Maruoka S, Horita S, Lee WC, Nagata K, Tanokura M J Mol Biol. 2010 Jan 15;395(2):417-29. Epub 2009 Nov 10. PMID:19900465[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maruoka S, Horita S, Lee WC, Nagata K, Tanokura M. Crystal structure of the ATPPase subunit and its substrate-dependent association with the GATase subunit: a novel regulatory mechanism for a two-subunit-type GMP synthetase from Pyrococcus horikoshii OT3. J Mol Biol. 2010 Jan 15;395(2):417-29. Epub 2009 Nov 10. PMID:19900465 doi:10.1016/j.jmb.2009.10.053
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