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1ht3

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[[Image:1ht3.jpg|left|200px]]<br /><applet load="1ht3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ht3.jpg|left|200px]]
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caption="1ht3, resolution 1.8&Aring;" />
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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 />
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{{Structure
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|PDB= 1ht3 |SIZE=350|CAPTION= <scene name='initialview01'>1ht3</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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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'''
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==Overview==
==Overview==
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==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 <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].
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1HT3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HT3 OCA].
==Reference==
==Reference==
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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., 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11886076 11886076]
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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., 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:[http://www.ncbi.nlm.nih.gov/pubmed/11886076 11886076]
[[Category: Engyodontium album]]
[[Category: Engyodontium album]]
[[Category: Peptidase K]]
[[Category: Peptidase K]]
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[[Category: stereochemistry]]
[[Category: stereochemistry]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:41:18 2008''

Revision as of 09:41, 20 March 2008

Image:1ht3.jpg


PDB ID 1ht3

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: and
Activity: Peptidase K, with EC number 3.4.21.64
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Thu Mar 20 11:41:18 2008

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