2qk4: Difference between revisions

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[[Image:2qk4.gif|left|200px]]<br /><applet load="2qk4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2qk4, resolution 2.45&Aring;" />
'''Human glycinamide ribonucleotide synthetase'''<br />


==About this Structure==
==Human glycinamide ribonucleotide synthetase==
2QK4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QK4 OCA].  
<StructureSection load='2qk4' size='340' side='right'caption='[[2qk4]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<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='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='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='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>
== Function ==
[https://www.uniprot.org/uniprot/PUR2_HUMAN PUR2_HUMAN]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=2qk4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:20631005</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2qk4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoribosylamine--glycine ligase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Arrowsmith CH]]
[[Category: Arrowsmith, C H.]]
[[Category: Berglund H]]
[[Category: Berg, S van den.]]
[[Category: Busam R]]
[[Category: Berglund, H.]]
[[Category: Collins R]]
[[Category: Busam, R.]]
[[Category: Dahlgren LG]]
[[Category: Collins, R.]]
[[Category: Edwards A]]
[[Category: Dahlgren, L G.]]
[[Category: Flodin S]]
[[Category: Edwards, A.]]
[[Category: Flores A]]
[[Category: Flodin, S.]]
[[Category: Graslund S]]
[[Category: Flores, A.]]
[[Category: Hallberg BM]]
[[Category: Graslund, S.]]
[[Category: Hammarstrom M]]
[[Category: Hallberg, B M.]]
[[Category: Herman MD]]
[[Category: Hammarstrom, M.]]
[[Category: Holmberg-Schiavone L]]
[[Category: Herman, M D.]]
[[Category: Johansson I]]
[[Category: Holmberg-Schiavone, L.]]
[[Category: Kallas A]]
[[Category: Johansson, I.]]
[[Category: Karlberg T]]
[[Category: Kallas, A.]]
[[Category: Kotenyova T]]
[[Category: Karlberg, T.]]
[[Category: Lehtio L]]
[[Category: Kotenyova, T.]]
[[Category: Moche M]]
[[Category: Lehtio, L.]]
[[Category: Nordlund P]]
[[Category: Moche, M.]]
[[Category: Nyman T]]
[[Category: Nordlund, P.]]
[[Category: Persson C]]
[[Category: Nyman, T.]]
[[Category: Sagemark J]]
[[Category: Persson, C.]]
[[Category: Stenmark P]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Sundstrom M]]
[[Category: Sagemark, J.]]
[[Category: Thorsell AG]]
[[Category: Stenmark, P.]]
[[Category: Tresaugues L]]
[[Category: Sundstrom, M.]]
[[Category: Weigelt J]]
[[Category: Thorsell, A G.]]
[[Category: Welin M]]
[[Category: Tresaugues, L.]]
[[Category: Van den Berg S]]
[[Category: Weigelt, J.]]
[[Category: Welin, M.]]
[[Category: ATP]]
[[Category: CL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: enzyme]]
[[Category: protein-atp complex]]
[[Category: purine synthesis]]
[[Category: sgc]]
[[Category: structural genomics]]
[[Category: structural genomics consortium]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:39:54 2008''

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

Drag the structure with the mouse to rotate

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