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[[Image:2id8.gif|left|200px]]
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{{STRUCTURE_2id8|  PDB=2id8  |  SCENE=  }}
'''Crystal structure of Proteinase K'''


==Crystal structure of Proteinase K==
<StructureSection load='2id8' size='340' side='right'caption='[[2id8]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2id8]] 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=2ID8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ID8 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]] 1.27&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2DB:(S)-(2,3-DIHYDROXYPROPOXY)TRIHYDROXYBORATE'>2DB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=2id8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2id8 OCA], [https://pdbe.org/2id8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2id8 RCSB], [https://www.ebi.ac.uk/pdbsum/2id8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2id8 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/id/2id8_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=2id8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
X-ray single-wavelength anomalous diffraction (SAD) data from a crystal of proteinase K were collected using synchrotron radiation of 0.98 A wavelength at SER-CAT 22-ID beamline, Advanced Photon Source, Argonne National Laboratory. At this wavelength, the expected Bijvoet ratio resulting from the presence of one calcium, one chloride and ten S atoms in the 279-residue protein is extremely small at approximately 0.46%. The direct-methods program SHELXD located 11 anomalous sites using data truncated to 2 A resolution. SHELXE was used to produce an easily interpretable electron-density map. This study shows that an accurate beamline and a good-quality crystal provide the possibility of successfully using a very weak anomalous signal of sulfur measured at a short wavelength for phasing a protein structure, even if a small degree of radiation damage is present.


==Overview==
What can be done with a good crystal and an accurate beamline?,Wang J, Dauter M, Dauter Z Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1475-83. Epub 2006, Nov 23. PMID:17139083<ref>PMID:17139083</ref>
X-ray single-wavelength anomalous diffraction (SAD) data from a crystal of proteinase K were collected using synchrotron radiation of 0.98 A wavelength at SER-CAT 22-ID beamline, Advanced Photon Source, Argonne National Laboratory. At this wavelength, the expected Bijvoet ratio resulting from the presence of one calcium, one chloride and ten S atoms in the 279-residue protein is extremely small at approximately 0.46%. The direct-methods program SHELXD located 11 anomalous sites using data truncated to 2 A resolution. SHELXE was used to produce an easily interpretable electron-density map. This study shows that an accurate beamline and a good-quality crystal provide the possibility of successfully using a very weak anomalous signal of sulfur measured at a short wavelength for phasing a protein structure, even if a small degree of radiation damage is present.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2ID8 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=2ID8 OCA].
</div>
<div class="pdbe-citations 2id8" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
What can be done with a good crystal and an accurate beamline?, Wang J, Dauter M, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1475-83. Epub 2006, Nov 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17139083 17139083]
*[[Proteinase 3D structures|Proteinase 3D structures]]
[[Category: Engyodontium album]]
== References ==
[[Category: Peptidase K]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Dauter, M.]]
</StructureSection>
[[Category: Dauter, Z.]]
[[Category: Large Structures]]
[[Category: Wang, J.]]
[[Category: Parengyodontium album]]
[[Category: Proteinase]]
[[Category: Dauter M]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:21:42 2008''
[[Category: Dauter Z]]
[[Category: Wang J]]
Retrieved from "https://proteopedia.org/2id8"