4fkc

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==Recombinant prolidase from Thermococcus sibiricus==
==Recombinant prolidase from Thermococcus sibiricus==
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<StructureSection load='4fkc' size='340' side='right' caption='[[4fkc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='4fkc' size='340' side='right'caption='[[4fkc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fkc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thesm Thesm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FKC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FKC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fkc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_sibiricus_MM_739 Thermococcus sibiricus MM 739]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FKC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TSIB_0821 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=604354 THESM])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
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<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=4fkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkc OCA], [http://pdbe.org/4fkc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fkc RCSB], [http://www.ebi.ac.uk/pdbsum/4fkc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fkc ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fkc OCA], [https://pdbe.org/4fkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fkc RCSB], [https://www.ebi.ac.uk/pdbsum/4fkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fkc ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/C6A2N7_THESM C6A2N7_THESM]
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Prolidases are peptidases that are specific for dipeptides with proline as the second residue. The structure of recombinant prolidase from the hyperthermophilic archaeon Thermococcus sibiricus (Tsprol) was determined at 2.6 A resolution. The homodimer of Tsprol is characterized by a complete lack of interactions between the N- and C-terminal domains of the two subunits and hence can be considered to be the most open structure when compared with previously structurally studied prolidases. This structure exists owing to intermolecular coordination bonds between cadmium ions derived from the crystallization solution and histidine residues of a His tag and aspartate and glutamate residues, which link the dimers to each other. This linking leads to the formation of a crystal with a loose packing of protein molecules and low resistance to mechanical influence and temperature increase.
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Influence of intermolecular contacts on the structure of recombinant prolidase from Thermococcus sibiricus.,Trofimov AA, Slutskaya EA, Polyakov KM, Dorovatovskii PV, Gumerov VM, Popov VO Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1275-8., doi: 10.1107/S174430911203761X. Epub 2012 Oct 26. PMID:23143231<ref>PMID:23143231</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4fkc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Aminopeptidase|Aminopeptidase]]
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Thesm]]
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[[Category: Large Structures]]
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[[Category: Dorovatovskii, P V]]
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[[Category: Thermococcus sibiricus MM 739]]
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[[Category: Gumerov, V M]]
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[[Category: Dorovatovskii PV]]
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[[Category: Polyakov, K M]]
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[[Category: Gumerov VM]]
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[[Category: Popov, V O]]
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[[Category: Polyakov KM]]
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[[Category: Slutskaya, E S]]
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[[Category: Popov VO]]
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[[Category: Trofimov, A A]]
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[[Category: Slutskaya ES]]
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[[Category: Hydrolase]]
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[[Category: Trofimov AA]]
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[[Category: Pita-bread structure]]
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[[Category: Prolidase]]
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Current revision

Recombinant prolidase from Thermococcus sibiricus

PDB ID 4fkc

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