View source for 1umz


==Xyloglucan endotransglycosylase in complex with the xyloglucan nonasaccharide XLLG.==
<StructureSection load='1umz' size='340' side='right'caption='[[1umz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1umz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_tremula Populus tremula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMZ 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</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=1umz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umz OCA], [https://pdbe.org/1umz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umz RCSB], [https://www.ebi.ac.uk/pdbsum/1umz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/XTH34_POPPZ XTH34_POPPZ] Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers (PubMed:12595718, PubMed:15020748, PubMed:15125664, PubMed:15804235, PubMed:16014999). Does not catalyze xyloglucan endohydrolysis (XEH) (PubMed:15804235). Involved in early phases of secondary (S) cell wall formation in fibers of the xylem and phloem vascular tissues of wood stems. May play a role in restructuring primary cell walls, possibly creating and reinforcing the connections between the primary and S cell wall layers (PubMed:12468728). Functions in the gelatinous (G) layers of the tension wood fibers that are involved in bending of the wood stems. May play a role in G fiber shrinking by repairing broken xyloglucan cross-links between G and S2 cell wall layers via its XET activity to maintain connections between the layers (PubMed:17504814).<ref>PMID:12468728</ref> <ref>PMID:12595718</ref> <ref>PMID:15020748</ref> <ref>PMID:15125664</ref> <ref>PMID:15804235</ref> <ref>PMID:16014999</ref> <ref>PMID:17504814</ref> 
== 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/um/1umz_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1umz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers in plant cell walls via a transglycosylation mechanism. Thus, XET is a key enzyme in all plant processes that require cell wall remodeling. To provide a basis for detailed structure-function studies, the crystal structure of Populus tremula x tremuloides XET16A (PttXET16A), heterologously expressed in Pichia pastoris, has been determined at 1.8-A resolution. Even though the overall structure of PttXET16A is a curved beta-sandwich similar to other enzymes in the glycoside hydrolase family GH16, parts of its substrate binding cleft are more reminiscent of the distantly related family GH7. In addition, XET has a C-terminal extension that packs against the conserved core, providing an additional beta-strand and a short alpha-helix. The structure of XET in complex with a xyloglucan nonasaccharide, XLLG, reveals a very favorable acceptor binding site, which is a necessary but not sufficient prerequisite for transglycosylation. Biochemical data imply that the enzyme requires sugar residues in both acceptor and donor sites to properly orient the glycosidic bond relative to the catalytic residues.

Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding.,Johansson P, Brumer H 3rd, Baumann MJ, Kallas AM, Henriksson H, Denman SE, Teeri TT, Jones TA Plant Cell. 2004 Apr;16(4):874-86. Epub 2004 Mar 12. PMID:15020748<ref>PMID:15020748</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1umz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Populus tremula]]
[[Category: Brumer H]]
[[Category: Denman SE]]
[[Category: Henriksson H]]
[[Category: Johansson P]]
[[Category: Jones TA]]
[[Category: Kallas AM]]
[[Category: Teeri TT]]