6fjs: Difference between revisions

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==Proteinase~K SIRAS phased structure of room-temperature, serially collected synchrotron data==
==Proteinase~K SIRAS phased structure of room-temperature, serially collected synchrotron data==
<StructureSection load='6fjs' size='340' side='right' caption='[[6fjs]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6fjs' size='340' side='right'caption='[[6fjs]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6fjs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FJS FirstGlance]. <br>
<table><tr><td colspan='2'>[[6fjs]] 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=6FJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FJS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fjs OCA], [http://pdbe.org/6fjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fjs RCSB], [http://www.ebi.ac.uk/pdbsum/6fjs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fjs ProSAT]</span></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=6fjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fjs OCA], [https://pdbe.org/6fjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fjs RCSB], [https://www.ebi.ac.uk/pdbsum/6fjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fjs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ]] Hydrolyzes keratin at aromatic and hydrophobic residues.  
[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6fjs" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6fjs" style="background-color:#fffaf0;"></div>
==See Also==
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Parengyodontium album]]
[[Category: Parengyodontium album]]
[[Category: Peptidase K]]
[[Category: Baitan D]]
[[Category: Baitan, D]]
[[Category: Betzel C]]
[[Category: Betzel, C]]
[[Category: Botha S]]
[[Category: Botha, S]]
[[Category: Chapman HN]]
[[Category: Chapman, H N]]
[[Category: Jungnickel KEJ]]
[[Category: Jungnickel, K E.J]]
[[Category: Oberthuer D]]
[[Category: Oberthuer, D]]
[[Category: Perbandt M]]
[[Category: Perbandt, M]]
[[Category: Schmidt C]]
[[Category: Schmidt, C]]
[[Category: Stern S]]
[[Category: Stern, S]]
[[Category: Wiedorn MO]]
[[Category: Wiedorn, M O]]
[[Category: Hydrolase]]
[[Category: Protease]]
[[Category: Serine protease]]

Latest revision as of 15:38, 6 November 2024

Proteinase~K SIRAS phased structure of room-temperature, serially collected synchrotron dataProteinase~K SIRAS phased structure of room-temperature, serially collected synchrotron data

Structural highlights

6fjs is a 1 chain structure with sequence from Parengyodontium album. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues.

Publication Abstract from PubMed

During the past few years, serial crystallography methods have undergone continuous development and serial data collection has become well established at high-intensity synchrotron-radiation beamlines and XFEL radiation sources. However, the application of experimental phasing to serial crystallography data has remained a challenging task owing to the inherent inaccuracy of the diffraction data. Here, a particularly gentle method for incorporating heavy atoms into micrometre-sized crystals utilizing lipidic cubic phase (LCP) as a carrier medium is reported. Soaking in LCP prior to data collection offers a new, efficient and gentle approach for preparing heavy-atom-derivative crystals directly before diffraction data collection using serial crystallography methods. This approach supports effective phasing by utilizing a reasonably low number of diffraction patterns. Using synchrotron radiation and exploiting the anomalous scattering signal of mercury for single isomorphous replacement with anomalous scattering (SIRAS) phasing resulted in high-quality electron-density maps that were sufficient for building a complete structural model of proteinase K at 1.9 A resolution using automatic model-building tools.

De novo protein structure determination by heavy-atom soaking in lipidic cubic phase and SIRAS phasing using serial synchrotron crystallography.,Botha S, Baitan D, Jungnickel KEJ, Oberthur D, Schmidt C, Stern S, Wiedorn MO, Perbandt M, Chapman HN, Betzel C IUCrJ. 2018 Aug 8;5(Pt 5):524-530. doi: 10.1107/S2052252518009223. eCollection, 2018 Sep 1. PMID:30224955[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Botha S, Baitan D, Jungnickel KEJ, Oberthur D, Schmidt C, Stern S, Wiedorn MO, Perbandt M, Chapman HN, Betzel C. De novo protein structure determination by heavy-atom soaking in lipidic cubic phase and SIRAS phasing using serial synchrotron crystallography. IUCrJ. 2018 Aug 8;5(Pt 5):524-530. doi: 10.1107/S2052252518009223. eCollection, 2018 Sep 1. PMID:30224955 doi:http://dx.doi.org/10.1107/S2052252518009223

6fjs, resolution 1.90Å

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OCA