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New page: left|200px<br /> <applet load="1jvd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jvd, resolution 2.40Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1jvd.gif|left|200px]]<br />
<applet load="1jvd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jvd, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN AGX2 COMPLEXED WITH UDPGLCNAC'''<br />


==Overview==
==CRYSTAL STRUCTURE OF HUMAN AGX2 COMPLEXED WITH UDPGLCNAC==
The recently published human genome with its relatively modest number of, genes has highlighted the importance of post-transcriptional and, post-translational modifications, such as alternative splicing or, glycosylation, in generating the complexities of human biology. The human, UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylases AGX1 and AGX2, which differ in sequence by an alternatively spliced 17 residue peptide, are key enzymes synthesizing UDPGlcNAc, an essential precursor for protein, glycosylation. To better understand the catalytic mechanism of these, enzymes and the role of the alternatively spliced segment, we have solved, the crystal structures of AGX1 and AGX2 in complexes with UDPGlcNAc (at, 1.9 and 2.4 A resolution, respectively) and UDPGalNAc (at 2.2 and 2.3 A, resolution, respectively). Comparison with known structures classifies, AGX1 and AGX2 as two new members of the SpsA-GnT I Core superfamily and, together with mutagenesis analysis, helps identify residues critical for, catalysis. Most importantly, our combined structural and biochemical data, provide evidence for a change in the oligomeric assembly accompanied by a, significant modification of the active site architecture, a result, suggesting that the two isoforms generated by alternative splicing may, have distinct catalytic properties.
<StructureSection load='1jvd' size='340' side='right'caption='[[1jvd]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1jvd]] 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=1JVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JVD FirstGlance]. <br>
1JVD 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 UD1 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JVD OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvd OCA], [https://pdbe.org/1jvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jvd RCSB], [https://www.ebi.ac.uk/pdbsum/1jvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvd ProSAT]</span></td></tr>
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture., Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y, EMBO J. 2001 Nov 15;20(22):6191-202. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11707391 11707391]
</table>
== Function ==
[https://www.uniprot.org/uniprot/UAP1_HUMAN UAP1_HUMAN] Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.
== 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/jv/1jvd_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=1jvd ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: UDP-N-acetylglucosamine diphosphorylase]]
[[Category: Bourne Y]]
[[Category: Bourne, Y.]]
[[Category: Peneff C]]
[[Category: Peneff, C.]]
[[Category: UD1]]
[[Category: alternative splicing]]
[[Category: nucleotidyltransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:44:51 2007''

Latest revision as of 13:25, 13 March 2024

CRYSTAL STRUCTURE OF HUMAN AGX2 COMPLEXED WITH UDPGLCNAC

1jvd, resolution 2.40Å

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