1azk: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1azk.gif|left|200px]]<br /><applet load="1azk" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1azk.gif|left|200px]]
caption="1azk" />
 
'''THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURES'''<br />
{{Structure
|PDB= 1azk |SIZE=350|CAPTION= <scene name='initialview01'>1azk</scene>
|SITE=  
|LIGAND=  
|ACTIVITY= [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91]
|GENE=
}}
 
'''THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURES'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
1AZK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZK OCA].  
1AZK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZK OCA].  


==Reference==
==Reference==
Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei., Mattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T, Protein Sci. 1997 Feb;6(2):294-303. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9041630 9041630]
Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei., Mattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T, Protein Sci. 1997 Feb;6(2):294-303. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9041630 9041630]
[[Category: Cellulose 1,4-beta-cellobiosidase]]
[[Category: Cellulose 1,4-beta-cellobiosidase]]
[[Category: Hypocrea jecorina]]
[[Category: Hypocrea jecorina]]
Line 22: Line 31:
[[Category: protein-carbohydrate interaction]]
[[Category: protein-carbohydrate interaction]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:54 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:17 2008''

Revision as of 11:04, 20 March 2008

File:1azk.gif


PDB ID 1azk

Drag the structure with the mouse to rotate
Activity: Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91
Coordinates: save as pdb, mmCIF, xml



THREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 19 STRUCTURES


OverviewOverview

Three-dimensional solution structures for three engineered, synthetic CBDs (Y5A, Y31A, and Y32A) of cellobiohydrolase I (CBHI) from Trichoderma reesei were studied with nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy. According to CD measurements the antiparallel beta-sheet structure of the CBD fold was preserved in all engineered peptides. The three-dimensional NMR-based structures of Y31A and Y32A revealed only small local changes due to mutations in the flat face of CBD, which is expected to bind to crystalline cellulose. Therefore, the structural roles of Y31 and Y32 are minor, but their functional importance is obvious because these mutants do not bind strongly to cellulose. In the case of Y5A, the disruption of the structural framework at the N-terminus and the complete loss of binding affinity implies that Y5 has both structural and functional significance. The number of aromatic residues and their precise spatial arrangement in the flat face of the type I CBD fold appears to be critical for specific binding. A model for the CBD binding in which the three aligned aromatic rings stack onto every other glucose ring of the cellulose polymer is discussed.

About this StructureAbout this Structure

1AZK is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei., Mattinen ML, Kontteli M, Kerovuo J, Linder M, Annila A, Lindeberg G, Reinikainen T, Drakenberg T, Protein Sci. 1997 Feb;6(2):294-303. PMID:9041630

Page seeded by OCA on Thu Mar 20 10:04:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA