1umz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1umz.gif|left|200px]]<br /><applet load="1umz" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1umz.gif|left|200px]]
-
caption="1umz, resolution 1.80&Aring;" />
+
 
-
'''XYLOGLUCAN ENDOTRANSGLYCOSYLASE IN COMPLEX WITH THE XYLOGLUCAN NONASACCHARIDE XLLG.'''<br />
+
{{Structure
 +
|PDB= 1umz |SIZE=350|CAPTION= <scene name='initialview01'>1umz</scene>, resolution 1.80&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Gal+Binding+Site+For+Chain+B'>AC1</scene>
 +
|LIGAND=
 +
|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]
 +
|GENE=
 +
}}
 +
 
 +
'''XYLOGLUCAN ENDOTRANSGLYCOSYLASE IN COMPLEX WITH THE XYLOGLUCAN NONASACCHARIDE XLLG.'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1UMZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Populus_tremula Populus tremula]. 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:Gal+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMZ OCA].
+
1UMZ 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=1UMZ OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15020748 15020748]
+
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]]
Line 30: Line 39:
[[Category: xyloglucan]]
[[Category: xyloglucan]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:19 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:34:06 2008''

Revision as of 12:34, 20 March 2008


PDB ID 1umz

Drag the structure with the mouse to rotate
, resolution 1.80Å
Sites:
Activity: Xyloglucan:xyloglucosyl transferase, with EC number 2.4.1.207
Coordinates: save as pdb, mmCIF, xml



XYLOGLUCAN ENDOTRANSGLYCOSYLASE IN COMPLEX WITH THE XYLOGLUCAN NONASACCHARIDE XLLG.


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

1UMZ 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

Page seeded by OCA on Thu Mar 20 14:34:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools