2b4f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2b4f.gif|left|200px]]<br /><applet load="2b4f" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2b4f.gif|left|200px]]
-
caption="2b4f, resolution 1.95&Aring;" />
+
 
-
'''Structure Of A Cold-Adapted Family 8 Xylanase in complex with substrate'''<br />
+
{{Structure
 +
|PDB= 2b4f |SIZE=350|CAPTION= <scene name='initialview01'>2b4f</scene>, resolution 1.95&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8]
 +
|GENE=
 +
}}
 +
 
 +
'''Structure Of A Cold-Adapted Family 8 Xylanase in complex with substrate'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2B4F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudoalteromonas_haloplanktis Pseudoalteromonas haloplanktis]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4F OCA].
+
2B4F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudoalteromonas_haloplanktis Pseudoalteromonas haloplanktis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B4F OCA].
==Reference==
==Reference==
-
Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product., De Vos D, Collins T, Nerinckx W, Savvides SN, Claeyssens M, Gerday C, Feller G, Van Beeumen J, Biochemistry. 2006 Apr 18;45(15):4797-807. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16605248 16605248]
+
Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product., De Vos D, Collins T, Nerinckx W, Savvides SN, Claeyssens M, Gerday C, Feller G, Van Beeumen J, Biochemistry. 2006 Apr 18;45(15):4797-807. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16605248 16605248]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Endo-1,4-beta-xylanase]]
[[Category: Pseudoalteromonas haloplanktis]]
[[Category: Pseudoalteromonas haloplanktis]]
Line 27: Line 36:
[[Category: xylan degradation]]
[[Category: xylan degradation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:02 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:57:23 2008''

Revision as of 13:57, 20 March 2008


PDB ID 2b4f

Drag the structure with the mouse to rotate
, resolution 1.95Å
Activity: Endo-1,4-beta-xylanase, with EC number 3.2.1.8
Coordinates: save as pdb, mmCIF, xml



Structure Of A Cold-Adapted Family 8 Xylanase in complex with substrate


Overview

The structures of inactive mutants D144A and E78Q of the glycoside hydrolase family 8 (GH-8) endo-beta-1,4-d-xylanase (pXyl) from the Antarctic bacterium Pseudoalteromonas haloplanktis TAH3a in complex with its substrate xylopentaose (at 1.95 A resolution) and product xylotriose (at 1.9 A resolution) have been determined by X-ray crystallography. A detailed comparative analysis of these with the apo-enzyme and with other GH-8 structures indicates an induced fit mechanism upon ligand binding whereby a number of conformational changes and, in particular, a repositioning of the proton donor into a more catalytically competent position occurs. This has also allowed for the description of protein-ligand interactions in this enzyme and for the demarcation of subsites -3 to +3. An in-depth analysis of each of these subsites gives an insight into the structure-function relationship of this enzyme and the basis of xylose/glucose discrimination in family 8 glycoside hydrolases. Furthermore, the structure of the -1/+1 subsite spanning complex reveals that the substrate is distorted from its ground state conformation. Indeed, structural analysis and in silico docking studies indicate that substrate hydrolysis in GH-8 members is preceded by a conformational change, away from the substrate ground-state chair conformation, to a pretransition state local minimum (2)S(O) conformation.

About this Structure

2B4F is a Single protein structure of sequence from Pseudoalteromonas haloplanktis. Full crystallographic information is available from OCA.

Reference

Oligosaccharide binding in family 8 glycosidases: crystal structures of active-site mutants of the beta-1,4-xylanase pXyl from Pseudoaltermonas haloplanktis TAH3a in complex with substrate and product., De Vos D, Collins T, Nerinckx W, Savvides SN, Claeyssens M, Gerday C, Feller G, Van Beeumen J, Biochemistry. 2006 Apr 18;45(15):4797-807. PMID:16605248

Page seeded by OCA on Thu Mar 20 15:57:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools