View source for 5txw


==Structure of Pfp1 protease from Thermococcus thioreducens: large cell H3 crystal form==
<StructureSection load='5txw' size='340' side='right'caption='[[5txw]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5txw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_thioreducens Thermococcus thioreducens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TXW 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]] 1.86&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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=5txw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5txw OCA], [https://pdbe.org/5txw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5txw RCSB], [https://www.ebi.ac.uk/pdbsum/5txw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5txw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0Q2XKL6_9EURY A0A0Q2XKL6_9EURY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Pfp1 protease, a cysteine protease of unknown specificity from the hyperthermophilic archaeon Thermococcus thioreducens, was crystallized in two distinctive crystal forms: from concentrated citrate in one case and PEG in the other. X-ray data were collected from both crystal forms at room temperature to about 1.9 A resolution using a laboratory source and detector, and the structures were solved by molecular replacement using the Pfp1 protease from Pyrococcus horikoshii as the search model. In the T. thioreducens protease structures, Cys18 residues on adjacent molecules in the asymmetric units form intermolecular disulfide bonds, thereby yielding hexamers composed of three cross-linked, quasi-dyad-related dimers with crystallographically exact threefold axes and exhibiting almost exact 32 symmetry. The corresponding residue in P. horikoshii Pfp1 is Tyr18. An individual active site containing Cys100 and His101 also includes a Glu74 residue contributed by a quasi-twofold-related, non-cross-linked subunit. Two catalytic triads are therefore closely juxtaposed about the quasi-twofold axis at the interface of these subunits, and are relatively sequestered within the hexamer cavity. The cysteine in the active site is observed to be oxidized in both of the crystal forms that were studied.

The structure of the Pfp1 protease from the hyperthermophilic archaeon Thermococcus thioreducens in two crystal forms.,Larson SB, McPherson A Acta Crystallogr D Struct Biol. 2017 Sep 1;73(Pt 9):749-756. doi:, 10.1107/S2059798317010622. Epub 2017 Aug 15. PMID:28876238<ref>PMID:28876238</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5txw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermococcus thioreducens]]
[[Category: Larson SB]]
[[Category: McPherson A]]