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==Human glycinamide ribonucleotide synthetase== | ==Human glycinamide ribonucleotide synthetase== | ||
<StructureSection load='2qk4' size='340' side='right' caption='[[2qk4]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='2qk4' size='340' side='right'caption='[[2qk4]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2qk4]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2qk4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QK4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GART, PGFT, PRGS ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GART, PGFT, PRGS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoribosylamine--glycine_ligase Phosphoribosylamine--glycine ligase], with EC number [https://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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qk4 OCA], [https://pdbe.org/2qk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qk4 RCSB], [https://www.ebi.ac.uk/pdbsum/2qk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qk4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 33: | Line 33: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Phosphoribosylamine--glycine ligase]] | [[Category: Phosphoribosylamine--glycine ligase]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
Revision as of 11:22, 25 June 2021
Human glycinamide ribonucleotide synthetaseHuman glycinamide ribonucleotide synthetase
Structural highlights
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 PubMedHuman purine de novo synthesis pathway contains several multi-functional enzymes, one of which, tri-functional GART, contains three enzymatic activities in a single polypeptide chain. We have solved structures of two domains bearing separate catalytic functions: glycinamide ribonucleotide synthetase and aminoimidazole ribonucleotide synthetase. Structures are compared with those of homologous enzymes from prokaryotes and analyzed in terms of the catalytic mechanism. We also report small angle X-ray scattering models for the full-length protein. These models are consistent with the enzyme forming a dimer through the middle domain. The protein has an approximate seesaw geometry where terminal enzyme units display high mobility owing to flexible linker segments. This resilient seesaw shape may facilitate internal substrate/product transfer or forwarding to other enzymes in the pathway. Structural studies of tri-functional human GART.,Welin M, Grossmann JG, Flodin S, Nyman T, Stenmark P, Tresaugues L, Kotenyova T, Johansson I, Nordlund P, Lehtio L Nucleic Acids Res. 2010 Nov 1;38(20):7308-19. Epub 2010 Jul 14. PMID:20631005[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Human
- Large Structures
- Phosphoribosylamine--glycine ligase
- Arrowsmith, C H
- Berg, S van den
- Berglund, H
- Busam, R
- Collins, R
- Dahlgren, L G
- Edwards, A
- Flodin, S
- Flores, A
- Graslund, S
- Hallberg, B M
- Hammarstrom, M
- Herman, M D
- Holmberg-Schiavone, L
- Johansson, I
- Kallas, A
- Karlberg, T
- Kotenyova, T
- Lehtio, L
- Moche, M
- Nordlund, P
- Nyman, T
- Persson, C
- Structural genomic
- Sagemark, J
- Stenmark, P
- Sundstrom, M
- Thorsell, A G
- Tresaugues, L
- Weigelt, J
- Welin, M
- Enzyme
- Ligase
- Protein-atp complex
- Purine synthesis
- Sgc