7s4z: Difference between revisions

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<StructureSection load='7s4z' size='340' side='right'caption='[[7s4z]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='7s4z' size='340' side='right'caption='[[7s4z]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7s4z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S4Z FirstGlance]. <br>
<table><tr><td colspan='2'>[[7s4z]] 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=7S4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S4Z FirstGlance]. <br>
</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=NO3:NITRATE+ION'>NO3</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7s4w|7s4w]], [[7s4r|7s4r]], [[7s4y|7s4y]]</div></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=NO3:NITRATE+ION'>NO3</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </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=7s4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s4z OCA], [https://pdbe.org/7s4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s4z RCSB], [https://www.ebi.ac.uk/pdbsum/7s4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s4z 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=7s4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s4z OCA], [https://pdbe.org/7s4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s4z RCSB], [https://www.ebi.ac.uk/pdbsum/7s4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s4z ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidase K]]
[[Category: Parengyodontium album]]
[[Category: Boer, R]]
[[Category: Boer R]]
[[Category: Botha, S]]
[[Category: Botha S]]
[[Category: Calisto, B]]
[[Category: Calisto B]]
[[Category: Carpena, X]]
[[Category: Carpena X]]
[[Category: Castellvi, A]]
[[Category: Castellvi A]]
[[Category: Crespo, I]]
[[Category: Crespo I]]
[[Category: Fromme, P]]
[[Category: Fromme P]]
[[Category: Gil, F]]
[[Category: Gil F]]
[[Category: Grieco, A]]
[[Category: Grieco A]]
[[Category: Hu, H]]
[[Category: Hu H]]
[[Category: Jernigan, R]]
[[Category: Jernigan R]]
[[Category: Ketawala, G]]
[[Category: Ketawala G]]
[[Category: Lisova, S]]
[[Category: Lisova S]]
[[Category: Martin-Garcia, J M]]
[[Category: Martin-Garcia JM]]
[[Category: Roy-Chowdbury, S]]
[[Category: Roy-Chowdbury S]]
[[Category: Spence, J]]
[[Category: Spence J]]
[[Category: Weierstall, U]]
[[Category: Weierstall U]]
[[Category: Zatsepin, N]]
[[Category: Zatsepin N]]
[[Category: Hydrolase]]
[[Category: Lcp injection]]
[[Category: Serial crystallography]]

Revision as of 19:44, 18 October 2023

Serial Macromolecular Crystallography at ALBA Synchrotron Light Source - Proteinase KSerial Macromolecular Crystallography at ALBA Synchrotron Light Source - Proteinase K

Structural highlights

7s4z 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

The increase in successful adaptations of serial crystallography at synchrotron radiation sources continues. To date, the number of serial synchrotron crystallography (SSX) experiments has grown exponentially, with over 40 experiments reported so far. In this work, we report the first SSX experiments with viscous jets conducted at ALBA beamline BL13-XALOC. Small crystals (15-30 microm) of five soluble proteins (lysozyme, proteinase K, phycocyanin, insulin and alpha-spectrin-SH3 domain) were suspended in lipidic cubic phase (LCP) and delivered to the X-ray beam with a high-viscosity injector developed at Arizona State University. Complete data sets were collected from all proteins and their high-resolution structures determined. The high quality of the diffraction data collected from all five samples, and the lack of specific radiation damage in the structures obtained in this study, confirm that the current capabilities at the beamline enables atomic resolution determination of protein structures from microcrystals as small as 15 microm using viscous jets at room temperature. Thus, BL13-XALOC can provide a feasible alternative to X-ray free-electron lasers when determining snapshots of macromolecular structures.

Serial macromolecular crystallography at ALBA Synchrotron Light Source.,Martin-Garcia JM, Botha S, Hu H, Jernigan R, Castellvi A, Lisova S, Gil F, Calisto B, Crespo I, Roy-Chowdhury S, Grieco A, Ketawala G, Weierstall U, Spence J, Fromme P, Zatsepin N, Boer DR, Carpena X J Synchrotron Radiat. 2022 May 1;29(Pt 3):896-907. doi:, 10.1107/S1600577522002508. Epub 2022 Apr 4. PMID:35511023[1]

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

See Also

References

  1. Martin-Garcia JM, Botha S, Hu H, Jernigan R, Castellvi A, Lisova S, Gil F, Calisto B, Crespo I, Roy-Chowdhury S, Grieco A, Ketawala G, Weierstall U, Spence J, Fromme P, Zatsepin N, Boer DR, Carpena X. Serial macromolecular crystallography at ALBA Synchrotron Light Source. J Synchrotron Radiat. 2022 May 1;29(Pt 3):896-907. doi:, 10.1107/S1600577522002508. Epub 2022 Apr 4. PMID:35511023 doi:http://dx.doi.org/10.1107/S1600577522002508

7s4z, resolution 1.90Å

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