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| | <StructureSection load='2yw2' size='340' side='right'caption='[[2yw2]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2yw2' size='340' side='right'caption='[[2yw2]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yw2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YW2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YW2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2yw2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YW2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gso|1gso]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoribosylamine--glycine_ligase Phosphoribosylamine--glycine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.13 6.3.4.13] </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=2yw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yw2 OCA], [https://pdbe.org/2yw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yw2 RCSB], [https://www.ebi.ac.uk/pdbsum/2yw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yw2 ProSAT], [https://www.topsan.org/Proteins/RSGI/2yw2 TOPSAN]</span></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=2yw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yw2 OCA], [http://pdbe.org/2yw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yw2 RCSB], [http://www.ebi.ac.uk/pdbsum/2yw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yw2 ProSAT], [http://www.topsan.org/Proteins/RSGI/2yw2 TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PUR2_AQUAE PUR2_AQUAE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquifex aeolicus huber and stetter 2001]] | + | [[Category: Aquifex aeolicus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoribosylamine--glycine ligase]]
| + | [[Category: Baba S]] |
| - | [[Category: Baba, S]] | + | [[Category: Kanagawa M]] |
| - | [[Category: Kanagawa, M]] | + | [[Category: Kawai G]] |
| - | [[Category: Kawai, G]] | + | [[Category: Kuramitsu S]] |
| - | [[Category: Kuramitsu, S]] | + | [[Category: Sampei G]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Yokoyama S]] |
| - | [[Category: Sampei, G]] | + | |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Atp binding]]
| + | |
| - | [[Category: Gar synthetase]]
| + | |
| - | [[Category: Glycinamide ribonucleotide synthetase]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Purine nucleotide biosynthetic pathway]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| Structural highlights
Function
PUR2_AQUAE
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
Glycinamide ribonucleotide synthetase (GAR-syn, PurD) catalyses the second reaction of the purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine and ATP to glycinamide ribonucleotide (GAR), ADP and Pi. In the present study, crystal structures of GAR-syn's from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus were determined in apo forms. Crystal structures in ligand-bound forms were also determined for G. kaustophilus and A. aeolicus proteins. In general, overall structures of GAR-syn's are similar to each other. However, the orientations of the B domains are varied among GAR-syn's and the MD simulation suggested the mobility of the B domain. Furthermore, it was demonstrated that the B loop in the B domain fixes the position of the beta- and gamma- phosphate groups of the bound ATP. The structures of GAR-syn's and the bound ligands were compared with each other in detail, and structures of GAR-syn's with full ligands, as well as the possible reaction mechanism, were proposed.
Crystal structures of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria.,Sampei G, Baba S, Kanagawa M, Yanai H, Ishii T, Kawai H, Fukai Y, Ebihara A, Nakagawa N, Kawai G J Biochem. 2010 Oct;148(4):429-38. Epub 2010 Aug 16. PMID:20716513[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sampei G, Baba S, Kanagawa M, Yanai H, Ishii T, Kawai H, Fukai Y, Ebihara A, Nakagawa N, Kawai G. Crystal structures of glycinamide ribonucleotide synthetase, PurD, from thermophilic eubacteria. J Biochem. 2010 Oct;148(4):429-38. Epub 2010 Aug 16. PMID:20716513 doi:10.1093/jb/mvq088
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