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1ht3

From Proteopedia

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[[Image:1ht3.jpg|left|200px]]
 
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{{Structure
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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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|PDB= 1ht3 |SIZE=350|CAPTION= <scene name='initialview01'>1ht3</scene>, resolution 1.8&Aring;
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<StructureSection load='1ht3' size='340' side='right'caption='[[1ht3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>
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<table><tr><td colspan='2'>[[1ht3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HT3 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ht3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ht3 OCA], [https://pdbe.org/1ht3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ht3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ht3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ht3 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1egq|1EGQ]], [[2prk|2PRK]], [[1cnm|1CNM]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ht3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ht3 OCA], [http://www.ebi.ac.uk/pdbsum/1ht3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ht3 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1ht3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ht3 ConSurf].
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<div style="clear:both"></div>
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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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==See Also==
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Large Structures]]
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[[Category: Parengyodontium album]]
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==About this Structure==
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[[Category: Gourinath S]]
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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].
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==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://www.ncbi.nlm.nih.gov/pubmed/11886076 11886076]
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[[Category: Engyodontium album]]
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[[Category: Peptidase K]]
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[[Category: Single protein]]
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[[Category: Gourinath, S.]]
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[[Category: mercury]]
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[[Category: proteinase k]]
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[[Category: stereochemistry]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:03 2008''
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Current revision

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

PDB ID 1ht3

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