1ht3: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ht3.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1ht3", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1ht3|  PDB=1ht3  |  SCENE=  }}
'''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'''


==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==
<StructureSection load='1ht3' size='340' side='right'caption='[[1ht3]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1ht3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:11886076</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1ht3" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Proteinase 3D structures|Proteinase 3D structures]]
[[Category: Engyodontium album]]
== References ==
[[Category: Peptidase K]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Gourinath, S.]]
</StructureSection>
[[Category: Mercury]]
[[Category: Large Structures]]
[[Category: Proteinase k]]
[[Category: Parengyodontium album]]
[[Category: Stereochemistry]]
[[Category: Gourinath S]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:12:13 2008''
Retrieved from "https://proteopedia.org/1ht3"