2qk4: Difference between revisions

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[[Image:2qk4.png|left|200px]]
==Human glycinamide ribonucleotide synthetase==
<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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QK4 FirstGlance]. <br>
</td></tr><tr><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><br>
<tr><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 Homo sapiens])</td></tr>
<tr><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><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://www.rcsb.org/pdb/explore.do?structureId=2qk4 RCSB], [http://www.ebi.ac.uk/pdbsum/2qk4 PDBsum]</span></td></tr>
<table>
== 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/chain_selection.php?pdb_ID=2ata 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.


{{STRUCTURE_2qk4|  PDB=2qk4  |  SCENE=  }}
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>


===Human glycinamide ribonucleotide synthetase===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_20631005}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2qk4]] is a 2 chain structure with sequence from [http://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].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:020631005</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoribosylamine--glycine ligase]]
[[Category: Phosphoribosylamine--glycine ligase]]

Revision as of 22:42, 30 September 2014

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.
Ligands:, , ,
Gene:GART, PGFT, PRGS (Homo sapiens)
Activity:Phosphoribosylamine--glycine ligase, with EC number 6.3.4.13
Resources:FirstGlance, OCA, RCSB, PDBsum

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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