2qk4: Difference between revisions

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==Human glycinamide ribonucleotide synthetase==
==Human glycinamide ribonucleotide synthetase==
<StructureSection load='2qk4' size='340' side='right' caption='[[2qk4]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='2qk4' size='340' side='right'caption='[[2qk4]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qk4]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QK4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2qk4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GART, PGFT, PRGS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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=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>
<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=2qk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qk4 OCA], [http://pdbe.org/2qk4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qk4 RCSB], [http://www.ebi.ac.uk/pdbsum/2qk4 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PUR2_HUMAN PUR2_HUMAN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/2qk4_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/2qk4_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qk4 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Phosphoribosylamine--glycine ligase]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Berg, S van den]]
[[Category: Berglund H]]
[[Category: Berglund, H]]
[[Category: Busam R]]
[[Category: Busam, R]]
[[Category: Collins R]]
[[Category: Collins, R]]
[[Category: Dahlgren LG]]
[[Category: Dahlgren, L G]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Flodin S]]
[[Category: Flodin, S]]
[[Category: Flores A]]
[[Category: Flores, A]]
[[Category: Graslund S]]
[[Category: Graslund, S]]
[[Category: Hallberg BM]]
[[Category: Hallberg, B M]]
[[Category: Hammarstrom M]]
[[Category: Hammarstrom, M]]
[[Category: Herman MD]]
[[Category: Herman, M D]]
[[Category: Holmberg-Schiavone L]]
[[Category: Holmberg-Schiavone, L]]
[[Category: Johansson I]]
[[Category: Johansson, I]]
[[Category: Kallas A]]
[[Category: Kallas, A]]
[[Category: Karlberg T]]
[[Category: Karlberg, T]]
[[Category: Kotenyova T]]
[[Category: Kotenyova, T]]
[[Category: Lehtio L]]
[[Category: Lehtio, L]]
[[Category: Moche M]]
[[Category: Moche, M]]
[[Category: Nordlund P]]
[[Category: Nordlund, P]]
[[Category: Nyman T]]
[[Category: Nyman, T]]
[[Category: Persson C]]
[[Category: Persson, C]]
[[Category: Sagemark J]]
[[Category: Structural genomic]]
[[Category: Stenmark P]]
[[Category: Sagemark, J]]
[[Category: Sundstrom M]]
[[Category: Stenmark, P]]
[[Category: Thorsell AG]]
[[Category: Sundstrom, M]]
[[Category: Tresaugues L]]
[[Category: Thorsell, A G]]
[[Category: Weigelt J]]
[[Category: Tresaugues, L]]
[[Category: Welin M]]
[[Category: Weigelt, J]]
[[Category: Van den Berg S]]
[[Category: Welin, M]]
[[Category: Enzyme]]
[[Category: Ligase]]
[[Category: Protein-atp complex]]
[[Category: Purine synthesis]]
[[Category: Sgc]]

Latest revision as of 14:34, 30 August 2023

Human glycinamide ribonucleotide synthetaseHuman glycinamide ribonucleotide synthetase

Structural highlights

2qk4 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.45Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PUR2_HUMAN

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

Human 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

  1. ↑ Welin M, Grossmann JG, Flodin S, Nyman T, Stenmark P, Tresaugues L, Kotenyova T, Johansson I, Nordlund P, Lehtio L. Structural studies of tri-functional human GART. Nucleic Acids Res. 2010 Nov 1;38(20):7308-19. Epub 2010 Jul 14. PMID:20631005 doi:10.1093/nar/gkq595

2qk4, resolution 2.45Å

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