1gct: Difference between revisions

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New page: left|200px<br /><applet load="1gct" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gct, resolution 1.6Å" /> '''IS GAMMA-CHYMOTRYPSIN...
 
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[[Image:1gct.gif|left|200px]]<br /><applet load="1gct" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1gct.gif|left|200px]]<br /><applet load="1gct" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1gct, resolution 1.6&Aring;" />
caption="1gct, resolution 1.6&Aring;" />
'''IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?'''<br />
'''IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?'''<br />


==Overview==
==Overview==
Refinement of the structure of gamma-chymotrypsin based on X-ray, crystallographic data to 1.6-A resolution has confirmed the overall, conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., &amp; Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In, addition, the new refinement suggests that gamma-chymotrypsin, which is, operationally defined by its crystalline habit, may not be the free enzyme, but rather a complex, possibly an acyl-enzyme adduct, with the, tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic, refinement provides a detailed geometrical description of the, enzyme-substrate-solvent interactions that occur in the presumptive, adduct.
Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., &amp; Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that gamma-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.


==About this Structure==
==About this Structure==
1GCT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GCT OCA].  
1GCT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCT OCA].  


==Reference==
==Reference==
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[[Category: Chymotrypsin]]
[[Category: Chymotrypsin]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Dixon, M.M.]]
[[Category: Dixon, M M.]]
[[Category: Matthews, B.W.]]
[[Category: Matthews, B W.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: hydrolase (serine proteinase)]]
[[Category: hydrolase (serine proteinase)]]


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