1z90

<table><tr><td colspan='2'>[[1z90]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z90 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z90 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2icx|2icx]], [[2icy|2icy]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AT3G03250 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z90 OCA], [http://pdbe.org/1z90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z90 RCSB], [http://www.ebi.ac.uk/pdbsum/1z90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z90 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/UGPA2_ARATH UGPA2_ARATH]] Plays a central role as a glucosyl donor in cellular metabolic pathways (By similarity).

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== Publication Abstract from PubMed ==

The structure of the UDP-glucose pyrophosphorylase encoded by Arabidopsis thaliana gene At3g03250 has been solved to a nominal resolution of 1.86 Angstroms. In addition, the structure has been solved in the presence of the substrates/products UTP and UDP-glucose to nominal resolutions of 1.64 Angstroms and 1.85 Angstroms. The three structures revealed a catalytic domain similar to that of other nucleotidyl-glucose pyrophosphorylases with a carboxy-terminal beta-helix domain in a unique orientation. Conformational changes are observed between the native and substrate-bound complexes. The nucleotide-binding loop and the carboxy-terminal domain, including the suspected catalytically important Lys360, move in and out of the active site in a concerted fashion. TLS refinement was employed initially to model conformational heterogeneity in the UDP-glucose complex followed by the use of multiconformer refinement for the entire molecule. Normal mode analysis generated atomic displacement predictions in good agreement in magnitude and direction with the observed conformational changes and anisotropic displacement parameters generated by TLS refinement. The structures and the observed dynamic changes provide insight into the ordered mechanism of this enzyme and previously described oligomerization effects on catalytic activity.

Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP.,McCoy JG, Bitto E, Bingman CA, Wesenberg GE, Bannen RM, Kondrashov DA, Phillips GN Jr J Mol Biol. 2007 Feb 23;366(3):830-41. Epub 2006 Nov 21. PMID:17178129<ref>PMID:17178129</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1z90" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Arath]]

[[Category: Allard, S T.M]]

[[Category: Bingman, C A]]

[[Category: Bitto, E]]

[[Category: Structural genomic]]

[[Category: Phillips, G N]]

[[Category: Wesenberg, G E]]

[[Category: Unknown function]]