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1ht3

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(New page: 200px<br /><applet load="1ht3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ht3, resolution 1.8&Aring;" /> '''MERCURY INDUCED MODIF...)
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'''MERCURY INDUCED MODIFICATIONS IN THE STEREOCHEMISTRY OF THE ACTIVE SITE THROUGH CYS-73 IN A SERINE PROTEASE: CRYSTAL STRUCTURE OF THE COMPLEX OF A PARTIALLY MODIFIED PROTEINASE K WITH MERCURY AT 1.8 A RESOLUTION'''<br />
'''MERCURY INDUCED MODIFICATIONS IN THE STEREOCHEMISTRY OF THE ACTIVE SITE THROUGH CYS-73 IN A SERINE PROTEASE: CRYSTAL STRUCTURE OF THE COMPLEX OF A PARTIALLY MODIFIED PROTEINASE K WITH MERCURY AT 1.8 A RESOLUTION'''<br />
==Overview==
==Overview==
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Proteinese K (PK) isolated from Tritirachium album Limber was crystallized, with HgCl2 in excess, under microgravity conditions. The intensity data, were collected at 4 degrees C to 1.8 A resolution and the final R-factor, after refinement for all the reflections was 0.164. Mercury has been found, at two sites with partial occupancies (0.4 and 0.6) which are at distances, of 2.48 A and 2.58 A respectively from Cys-73 Sgamma. The Cys-73 in the, enzyme structure is located close to the active site residue, His-69. This, region is completely buried and is not accessible to the solvent. It is, rather tightly packed. Therefore, the binding of mercury distorts the, stereochemistry of the neighbouring residues including those belonging to, the catalytic triad. As a result of this, the Ogamma of Ser-224 is, displaced by 0.6 A which causes the inactivation of proteinase K by, increasing the H-bond distance to 3.7 A between Ser-224 Ogamma and His-69, Nepsilon2.
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Proteinese K (PK) isolated from Tritirachium album Limber was crystallized with HgCl2 in excess, under microgravity conditions. The intensity data were collected at 4 degrees C to 1.8 A resolution and the final R-factor after refinement for all the reflections was 0.164. Mercury has been found at two sites with partial occupancies (0.4 and 0.6) which are at distances of 2.48 A and 2.58 A respectively from Cys-73 Sgamma. The Cys-73 in the enzyme structure is located close to the active site residue, His-69. This region is completely buried and is not accessible to the solvent. It is rather tightly packed. Therefore, the binding of mercury distorts the stereochemistry of the neighbouring residues including those belonging to the catalytic triad. As a result of this, the Ogamma of Ser-224 is displaced by 0.6 A which causes the inactivation of proteinase K by increasing the H-bond distance to 3.7 A between Ser-224 Ogamma and His-69 Nepsilon2.
==About this Structure==
==About this Structure==
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1HT3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album] with HG and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HT3 OCA].
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1HT3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album] with <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HT3 OCA].
==Reference==
==Reference==
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[[Category: stereochemistry]]
[[Category: stereochemistry]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:48:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:35 2008''

Revision as of 11:04, 21 February 2008

Image:1ht3.jpg

1ht3, resolution 1.8Å

Drag the structure with the mouse to rotate

MERCURY INDUCED MODIFICATIONS IN THE STEREOCHEMISTRY OF THE ACTIVE SITE THROUGH CYS-73 IN A SERINE PROTEASE: CRYSTAL STRUCTURE OF THE COMPLEX OF A PARTIALLY MODIFIED PROTEINASE K WITH MERCURY AT 1.8 A RESOLUTION

Overview

Proteinese K (PK) isolated from Tritirachium album Limber was crystallized with HgCl2 in excess, under microgravity conditions. The intensity data were collected at 4 degrees C to 1.8 A resolution and the final R-factor after refinement for all the reflections was 0.164. Mercury has been found at two sites with partial occupancies (0.4 and 0.6) which are at distances of 2.48 A and 2.58 A respectively from Cys-73 Sgamma. The Cys-73 in the enzyme structure is located close to the active site residue, His-69. This region is completely buried and is not accessible to the solvent. It is rather tightly packed. Therefore, the binding of mercury distorts the stereochemistry of the neighbouring residues including those belonging to the catalytic triad. As a result of this, the Ogamma of Ser-224 is displaced by 0.6 A which causes the inactivation of proteinase K by increasing the H-bond distance to 3.7 A between Ser-224 Ogamma and His-69 Nepsilon2.

About this Structure

1HT3 is a Single protein structure of sequence from Engyodontium album with and as ligands. Active as Peptidase K, with EC number 3.4.21.64 Full crystallographic information is available from OCA.

Reference

Mercury induced modifications in the stereochemistry of the active site through Cys-73 in a serine protease--crystal structure of the complex of a partially modified proteinase K with mercury at 1.8 A resolution., Gourinath S, Degenhardt M, Eschenburg S, Moore K, Delucas LJ, Betzel C, Singh TP, Indian J Biochem Biophys. 2001 Oct;38(5):298-302. PMID:11886076

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