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| | <StructureSection load='5ex1' size='340' side='right'caption='[[5ex1]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='5ex1' size='340' side='right'caption='[[5ex1]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ex1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Hirbi Hirbi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EX1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EX1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ex1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirschia_baltica_ATCC_49814 Hirschia baltica ATCC 49814]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EX1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.053Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hbal_3123 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=582402 HIRBI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ex1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ex1 OCA], [http://pdbe.org/5ex1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ex1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ex1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ex1 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=5ex1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ex1 OCA], [https://pdbe.org/5ex1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ex1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ex1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ex1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C6XII3_HIRBI C6XII3_HIRBI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hirbi]] | + | [[Category: Hirschia baltica ATCC 49814]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jakob, R P]] | + | [[Category: Jakob RP]] |
| - | [[Category: Maier, T]] | + | [[Category: Maier T]] |
| - | [[Category: Cyclophilin]]
| + | |
| - | [[Category: Folding helper]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Ppiase]]
| + | |
| - | [[Category: Rotamase]]
| + | |
| Structural highlights
Function
C6XII3_HIRBI
Publication Abstract from PubMed
Cyclophilins are ubiquitous cis-trans-prolyl isomerases (PPIases) found in all kingdoms of life. Here, we identify a novel family of cyclophilins, termed AquaCyps, which specifically occurs in marine Alphaproteobacteria, but not in related terrestric species. In addition to a canonical PPIase domain, AquaCyps contain large extensions and insertions. The crystal structures of two representatives from Hirschia baltica, AquaCyp293 and AquaCyp300, reveal the formation of a compact domain, the NIC domain, by the N- and C-terminal extensions together with a central insertion. The NIC domain adopts a novel mixed alpha-helical, beta-sheet fold that is linked to the cyclophilin domain via a conserved disulfide bond. In its overall fold, AquaCyp293 resembles AquaCyp300, but the two proteins utilize distinct sets of active site residues, consistent with differences in their PPIase catalytic properties. While AquaCyp293 is a highly active general PPIase, AquaCyp300 is specific for hydrophobic substrate peptides and exhibits lower overall activity.
Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.,Jakob RP, Schmidpeter PA, Koch JR, Schmid FX, Maier T PLoS One. 2016 Jun 8;11(6):e0157070. doi: 10.1371/journal.pone.0157070., eCollection 2016. PMID:27276069[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jakob RP, Schmidpeter PA, Koch JR, Schmid FX, Maier T. Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps. PLoS One. 2016 Jun 8;11(6):e0157070. doi: 10.1371/journal.pone.0157070., eCollection 2016. PMID:27276069 doi:http://dx.doi.org/10.1371/journal.pone.0157070
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