3aj9: Difference between revisions
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< | ==X-ray analysis of Crystal of Proteinase K Obtained from D2O Solution Using PEG 8000== | ||
<StructureSection load='3aj9' size='340' side='right'caption='[[3aj9]], [[Resolution|resolution]] 1.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3aj9]] 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=3AJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AJ9 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]] 1.1Å</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=GOL:GLYCEROL'>GOL</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=3aj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aj9 OCA], [https://pdbe.org/3aj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aj9 RCSB], [https://www.ebi.ac.uk/pdbsum/3aj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aj9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Deuteration of macromolecules is an important technique in neutron protein crystallography. Solvent deuteration of protein crystals is carried out by replacing water (H(2)O) with heavy water (D(2)O) prior to neutron diffraction experiments in order to diminish background noise. The effects of solvent deuteration on the crystallization of proteinase K (PK) with polyethylene glycol as a precipitant were investigated using high-resolution X-ray crystallography. In previous studies, eight NO(3)(-) anions were included in the PK crystal unit cell grown in NaNO(3) solution. In this study, however, the PK crystal structure did not contain NO(3)(-) anions; consequently, distortions of amino acids arising from the presence of NO(3)(-) anions were avoided in the present crystal structures. High-resolution (1.1 A) X-ray diffraction studies showed that the degradation of PK crystals induced by solvent deuteration was so small that this degradation would be negligible for the purpose of neutron protein crystallography experiments at medium resolution. Comparison of the nonhydrogen structures of nondeuterated and deuterated crystal structures demonstrated very small structural differences. Moreover, a positive correlation between the root-mean-squared differences and B factors indicated that no systematic difference existed. | |||
High-resolution X-ray study of the effects of deuteration on crystal growth and the crystal structure of proteinase K.,Chatake T, Ishikawa T, Yanagisawa Y, Yamada T, Tanaka I, Fujiwara S, Morimoro Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1334-8., Epub 2011 Oct 25. PMID:22102227<ref>PMID:22102227</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3aj9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Proteinase 3D structures|Proteinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[ | [[Category: Parengyodontium album]] | ||
[[Category: Chatake T]] | |||
== | [[Category: Ishikawa T]] | ||
< | [[Category: Morimoto Y]] | ||
[[Category: | |||
[[Category: | |||
[[Category: Chatake | |||
[[Category: Ishikawa | |||
[[Category: Morimoto | |||
Latest revision as of 17:29, 1 November 2023
X-ray analysis of Crystal of Proteinase K Obtained from D2O Solution Using PEG 8000X-ray analysis of Crystal of Proteinase K Obtained from D2O Solution Using PEG 8000
Structural highlights
FunctionPRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues. Publication Abstract from PubMedDeuteration of macromolecules is an important technique in neutron protein crystallography. Solvent deuteration of protein crystals is carried out by replacing water (H(2)O) with heavy water (D(2)O) prior to neutron diffraction experiments in order to diminish background noise. The effects of solvent deuteration on the crystallization of proteinase K (PK) with polyethylene glycol as a precipitant were investigated using high-resolution X-ray crystallography. In previous studies, eight NO(3)(-) anions were included in the PK crystal unit cell grown in NaNO(3) solution. In this study, however, the PK crystal structure did not contain NO(3)(-) anions; consequently, distortions of amino acids arising from the presence of NO(3)(-) anions were avoided in the present crystal structures. High-resolution (1.1 A) X-ray diffraction studies showed that the degradation of PK crystals induced by solvent deuteration was so small that this degradation would be negligible for the purpose of neutron protein crystallography experiments at medium resolution. Comparison of the nonhydrogen structures of nondeuterated and deuterated crystal structures demonstrated very small structural differences. Moreover, a positive correlation between the root-mean-squared differences and B factors indicated that no systematic difference existed. High-resolution X-ray study of the effects of deuteration on crystal growth and the crystal structure of proteinase K.,Chatake T, Ishikawa T, Yanagisawa Y, Yamada T, Tanaka I, Fujiwara S, Morimoro Y Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1334-8., Epub 2011 Oct 25. PMID:22102227[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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