1esa: Difference between revisions

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New page: left|200px<br /><applet load="1esa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esa, resolution 1.65Å" /> '''DIRECT STRUCTURE OBS...
 
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[[Image:1esa.gif|left|200px]]<br /><applet load="1esa" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1esa.gif|left|200px]]<br /><applet load="1esa" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1esa, resolution 1.65&Aring;" />
caption="1esa, resolution 1.65&Aring;" />
'''DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE'''<br />
'''DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE'''<br />


==Overview==
==Overview==
The method of X-ray crystallographic cryoenzymology has been used to, determine the crystal structure of a kinetically significant species on, the reaction pathway of a crystalline enzyme. The structure of a specific, acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of the, N-carbobenzoxy-L-alanine p-nitrophenyl ester has been determined and, refined against X-ray diffraction data at 2.3-A resolution. The difference, Fourier electron density map clearly shows electron density for the, trapped acyl-enzyme. The acyl-enzyme was formed at -26 degrees C and was, stabilized at -55 degrees C during data collection, taking advantage of, the glass transition in protein dynamics that occurs at around -50 degrees, C.
The method of X-ray crystallographic cryoenzymology has been used to determine the crystal structure of a kinetically significant species on the reaction pathway of a crystalline enzyme. The structure of a specific acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of the N-carbobenzoxy-L-alanine p-nitrophenyl ester has been determined and refined against X-ray diffraction data at 2.3-A resolution. The difference Fourier electron density map clearly shows electron density for the trapped acyl-enzyme. The acyl-enzyme was formed at -26 degrees C and was stabilized at -55 degrees C during data collection, taking advantage of the glass transition in protein dynamics that occurs at around -50 degrees C.


==About this Structure==
==About this Structure==
1ESA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESA OCA].  
1ESA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESA OCA].  


==Reference==
==Reference==
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Ding, X.]]
[[Category: Ding, X.]]
[[Category: Petsko, G.A.]]
[[Category: Petsko, G A.]]
[[Category: Rasmussen, B.]]
[[Category: Rasmussen, B.]]
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
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[[Category: hydrolase(serine proteinase)]]
[[Category: hydrolase(serine proteinase)]]


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