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1umz

From Proteopedia

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Current revision

Xyloglucan endotransglycosylase in complex with the xyloglucan nonasaccharide XLLG.

Structural highlights

1umz is a 2 chain structure with sequence from Populus tremula. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

XTH34_POPPZ Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers (PubMed:12595718, PubMed:15020748, PubMed:16014999, PubMed:15804235, PubMed:15125664). 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).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

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

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^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bourquin V, Nishikubo N, Abe H, Brumer H, Denman S, Eklund M, Christiernin M, Teeri TT, Sundberg B, Mellerowicz EJ. Xyloglucan endotransglycosylases have a function during the formation of secondary cell walls of vascular tissues. Plant Cell. 2002 Dec;14(12):3073-88. PMID:12468728 doi:10.1105/tpc.007773
↑ Johansson P, Denman S, Brumer H, Kallas AM, Henriksson H, Bergfors T, Teeri TT, Jones TA. Crystallization and preliminary X-ray analysis of a xyloglucan endotransglycosylase from Populus tremula x tremuloides. Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):535-7. PMID:12595718 doi:10.1107/s090744490202348x
↑ Johansson P, Brumer H 3rd, Baumann MJ, Kallas AM, Henriksson H, Denman SE, Teeri TT, Jones TA. Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding. Plant Cell. 2004 Apr;16(4):874-86. Epub 2004 Mar 12. PMID:15020748 doi:http://dx.doi.org/10.1105/tpc.020065
↑ Brumer H 3rd, Zhou Q, Baumann MJ, Carlsson K, Teeri TT. Activation of crystalline cellulose surfaces through the chemoenzymatic modification of xyloglucan. J Am Chem Soc. 2004 May 12;126(18):5715-21. PMID:15125664 doi:10.1021/ja0316770
↑ Kallas AM, Piens K, Denman SE, Henriksson H, Fäldt J, Johansson P, Brumer H, Teeri TT. Enzymatic properties of native and deglycosylated hybrid aspen (Populus tremulaxtremuloides) xyloglucan endotransglycosylase 16A expressed in Pichia pastoris. Biochem J. 2005 Aug 15;390(Pt 1):105-13. PMID:15804235 doi:10.1042/BJ20041749
↑ Bollok M, Henriksson H, Kallas A, Jahic M, Teeri TT, Enfors SO. Production of poplar xyloglucan endotransglycosylase using the methylotrophic yeast Pichia pastoris. Appl Biochem Biotechnol. 2005 Jul;126(1):61-77. PMID:16014999 doi:10.1007/s12010-005-0006-4
↑ Nishikubo N, Awano T, Banasiak A, Bourquin V, Ibatullin F, Funada R, Brumer H, Teeri TT, Hayashi T, Sundberg B, Mellerowicz EJ. Xyloglucan endo-transglycosylase (XET) functions in gelatinous layers of tension wood fibers in poplar--a glimpse into the mechanism of the balancing act of trees. Plant Cell Physiol. 2007 Jun;48(6):843-55. PMID:17504814 doi:10.1093/pcp/pcm055
↑ Johansson P, Brumer H 3rd, Baumann MJ, Kallas AM, Henriksson H, Denman SE, Teeri TT, Jones TA. Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding. Plant Cell. 2004 Apr;16(4):874-86. Epub 2004 Mar 12. PMID:15020748 doi:http://dx.doi.org/10.1105/tpc.020065

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1umz"

@@ Line 3: / Line 3: @@
 <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/European_aspen European aspen]. 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>
+<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='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=XYS:XYLOPYRANOSE'>XYS</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1un1|1un1]]</div></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Xyloglucan:xyloglucosyl_transferase Xyloglucan:xyloglucosyl transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.207 2.4.1.207] </span></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:16014999, PubMed:15804235, PubMed:15125664). 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]]
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: European aspen]]
 [[Category: Large Structures]]
-[[Category: Xyloglucan:xyloglucosyl transferase]]
+[[Category: Populus tremula]]
-[[Category: Brumer, H]]
+[[Category: Brumer H]]
-[[Category: Denman, S E]]
+[[Category: Denman SE]]
-[[Category: Henriksson, H]]
+[[Category: Henriksson H]]
-[[Category: Johansson, P]]
+[[Category: Johansson P]]
-[[Category: Jones, T A]]
+[[Category: Jones TA]]
-[[Category: Kallas, A M]]
+[[Category: Kallas AM]]
-[[Category: Teeri, T T]]
+[[Category: Teeri TT]]
-[[Category: Glycoside hydrolase]]
-[[Category: Glycosyltransferase]]
-[[Category: Transferase]]
-[[Category: Transglycosylation]]
-[[Category: Xeh]]
-[[Category: Xet]]
-[[Category: Xth]]
-[[Category: Xyloglucan]]

1umz

From Proteopedia

Current revision

Xyloglucan endotransglycosylase in complex with the xyloglucan nonasaccharide XLLG.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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