6cel: Difference between revisions

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[[Image:6cel.gif|left|200px]]<br /><applet load="6cel" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:6cel.gif|left|200px]]<br /><applet load="6cel" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="6cel, resolution 1.7&Aring;" />
caption="6cel, resolution 1.7&Aring;" />
'''CBH1 (E212Q) CELLOPENTAOSE COMPLEX'''<br />
'''CBH1 (E212Q) CELLOPENTAOSE COMPLEX'''<br />
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==About this Structure==
==About this Structure==
6CEL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with NAG and CO as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Sites: <scene name='pdbsite=CAT:Catalytic Site Including Mutation E212q'>CAT</scene> and <scene name='pdbsite=COB:Co-Binding Site On Crystallographic Dyad. The Metal Ion ...'>COB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=6CEL OCA].  
6CEL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=CO:'>CO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Known structural/functional Sites: <scene name='pdbsite=CAT:Catalytic+Site+Including+Mutation+E212q'>CAT</scene> and <scene name='pdbsite=COB:Co-Binding+Site+On+Crystallographic+Dyad.+The+Metal+Ion+...'>COB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CEL OCA].  


==Reference==
==Reference==
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[[Category: hydrolase]]
[[Category: hydrolase]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:53:37 2008''

Revision as of 11:53, 3 February 2008

File:6cel.gif


6cel, resolution 1.7Å

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CBH1 (E212Q) CELLOPENTAOSE COMPLEX

OverviewOverview

Detailed information has been obtained, by means of protein X-ray, crystallography, on how a cellulose chain is bound in the, cellulose-binding tunnel of cellobiohydrolase I (CBHI), the major, cellulase in the hydrolysis of native, crystalline cellulose by the fungus, Trichoderma reesei. Three high-resolution crystal structures of different, catalytically deficient mutants of CBHI in complex with cellotetraose, cellopentaose and cellohexaose have been refined at 1.9, 1.7 and 1.9 A, resolution, respectively. The observed binding of cellooligomers in the, tunnel allowed unambiguous identification of ten well-defined subsites for, glucosyl units that span a length of approximately 50 A. All bound, oligomers have the same directionality and orientation, and the positions, of the glucosyl units in each binding site agree remarkably well between, the different complexes. The binding mode observed here corresponds to, that expected during productive binding of a cellulose chain. The, structures support the hypothesis that hydrolysis by CBHI proceeds from, the reducing towards the non-reducing end of a cellulose chain, and they, provide a structural explanation for the observed distribution of initial, hydrolysis products.

About this StructureAbout this Structure

6CEL is a Single protein structure of sequence from Hypocrea jecorina with and as ligands. Active as Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

ReferenceReference

High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei., Divne C, Stahlberg J, Teeri TT, Jones TA, J Mol Biol. 1998 Jan 16;275(2):309-25. PMID:9466911

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