1un1

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[[Image:1un1.gif|left|200px]]<br /><applet load="1un1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1un1.gif|left|200px]]
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caption="1un1, resolution 2.10&Aring;" />
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'''XYLOGLUCAN ENDOTRANSGLYCOSYLASE NATIVE STRUCTURE.'''<br />
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{{Structure
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|PDB= 1un1 |SIZE=350|CAPTION= <scene name='initialview01'>1un1</scene>, resolution 2.10&Aring;
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|SITE= <scene name='pdbsite=AC1:Au+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=AU:GOLD ION'>AU</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Xyloglucan:xyloglucosyl_transferase Xyloglucan:xyloglucosyl transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.207 2.4.1.207]
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|GENE=
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}}
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'''XYLOGLUCAN ENDOTRANSGLYCOSYLASE NATIVE STRUCTURE.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UN1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Populus_tremula Populus tremula] with <scene name='pdbligand=AU:'>AU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Xyloglucan:xyloglucosyl_transferase Xyloglucan:xyloglucosyl transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.207 2.4.1.207] Known structural/functional Site: <scene name='pdbsite=AC1:Au+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN1 OCA].
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1UN1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Populus_tremula Populus tremula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UN1 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15020748 15020748]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15020748 15020748]
[[Category: Populus tremula]]
[[Category: Populus tremula]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: xyloglucan]]
[[Category: xyloglucan]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:34:08 2008''

Revision as of 12:34, 20 March 2008


PDB ID 1un1

Drag the structure with the mouse to rotate
, resolution 2.10Å
Sites:
Ligands:
Activity: Xyloglucan:xyloglucosyl transferase, with EC number 2.4.1.207
Coordinates: save as pdb, mmCIF, xml



XYLOGLUCAN ENDOTRANSGLYCOSYLASE NATIVE STRUCTURE.


Overview

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.

About this Structure

1UN1 is a Single protein structure of sequence from Populus tremula. Full crystallographic information is available from OCA.

Reference

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

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