From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1us3.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1us3.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1us3| PDB=1us3 | SCENE= }} | | {{STRUCTURE_1us3| PDB=1us3 | SCENE= }} |
| | | | |
| - | '''NATIVE XYLANASE10C FROM CELLVIBRIO JAPONICUS'''
| + | ===NATIVE XYLANASE10C FROM CELLVIBRIO JAPONICUS=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Microbial degradation of the plant cell wall is the primary mechanism by which carbon is utilized in the biosphere. The hydrolysis of xylan, by endo-beta-1,4-xylanases (xylanases), is one of the key reactions in this process. Although amino acid sequence variations are evident in the substrate binding cleft of "family GH10" xylanases (see afmb.cnrs-mrs.fr/CAZY/), their biochemical significance is unclear. The Cellvibrio japonicus GH10 xylanase CjXyn10C is a bi-modular enzyme comprising a GH10 catalytic module and a family 15 carbohydrate-binding module. The three-dimensional structure at 1.85 A, presented here, shows that the sequence joining the two modules is disordered, confirming that linker sequences in modular glycoside hydrolases are highly flexible. CjXyn10C hydrolyzes xylan at a rate similar to other previously described GH10 enzymes but displays very low activity against xylooligosaccharides. The poor activity on short substrates reflects weak binding at the -2 subsite of the enzyme. Comparison of CjXyn10C with other family GH10 enzymes reveals "polymorphisms" in the substrate binding cleft including a glutamate/glycine substitution at the -2 subsite and a tyrosine insertion in the -2/-3 glycone region of the substrate binding cleft, both of which contribute to the unusual properties of the enzyme. The CjXyn10C-substrate complex shows that Tyr-340 stacks against the xylose residue located at the -3 subsite, and the properties of Y340A support the view that this tyrosine plays a pivotal role in substrate binding at this location. The generic importance of using CjXyn10C as a template in predicting the biochemical properties of GH10 xylanases is discussed.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14670951}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14670951 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_14670951}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Xylan degradation]] | | [[Category: Xylan degradation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:36:48 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:00:07 2008'' |
Revision as of 13:00, 28 July 2008
Template:STRUCTURE 1us3
NATIVE XYLANASE10C FROM CELLVIBRIO JAPONICUS
Template:ABSTRACT PUBMED 14670951
About this Structure
1US3 is a Single protein structure of sequence from Cellvibrio japonicus. Full crystallographic information is available from OCA.
Reference
Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases., Pell G, Szabo L, Charnock SJ, Xie H, Gloster TM, Davies GJ, Gilbert HJ, J Biol Chem. 2004 Mar 19;279(12):11777-88. Epub 2003 Dec 11. PMID:14670951
Page seeded by OCA on Mon Jul 28 16:00:07 2008
